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BETA-HAIRPIN PEPTIDOMIMETICS

20210284693 · 2021-09-16

    Inventors

    Cpc classification

    International classification

    Abstract

    Beta-hairpin peptidomimetics of the general formula (I), and pharmaceutically acceptable salts thereof, with P, X, Q., and optionally L being elements as defined in the description and the claims, have Gram-negative antimicrobial activity to e.g. inhibit the growth or to kill microorganisms such as Klebsiella pneumoniae and/or Acinetobacterbaumannii and/or Escherichia coli and/or Pseudomonas aeruginosa and/or Enterobacter cloacae. They can be used as medicaments to treat or prevent infections or as disinfectants for foodstuffs, cosmetics, medicaments or other nutrient-containing materials. These peptidomimetics can be manufactured by a process which is based on a mixed solid- and solution phase synthetic strategy.

    Claims

    1. Compounds of the formula (I), ##STR00451## comprising a module A consisting of single elements P or X being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element wherein s=0, t=0, and u=0; or s=1, t=0, and u=0; or s=0, t=0, and u=1; or s=1, t=1, and u=0; or s=1, t=0, and u=1; or s=1, t=1, and u=1; if s=1, t=1, and u=1; and X.sup.14 and X.sup.13 taken together and/or P.sup.1 and X.sup.12 taken together and/or P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids or non-naturally cross-linking acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting X.sup.14 and X.sup.13 and/or P.sup.1 and X.sup.12 and/or P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then X.sup.14 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.1 is a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.2 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.3 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.4 is Gly; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.5 is Gly; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.6 is Gly; or a naturally or non-naturally occurring basic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or or one guanidino function; or a naturally or non-naturally occurring alcoholic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.7 is Gly; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.9 is Gly; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; P.sup.10 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.11 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; X.sup.12 is Gly; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; X.sup.13 is Glyol; or a naturally or non-naturally occurring aliphatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; with the proviso that, if P.sup.1 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; P.sup.m; or X.sup.12; is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid and if P.sup.10 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the combined number of interstrand linkages and salt bridges in above module A must not exceed two; if X.sup.14 and X.sup.13 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.1 and X.sup.12 taken together are not forming an interstrand linkage or salt bridge, as defined above; if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or a salt bridge, as defined above; the carbonyl (C═O) point of attachment of X.sup.13 and the nitrogen (N) point of attachment of X.sup.14 are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=1, t=0, and u=1; and P.sup.1 and X.sup.12 taken together and/or P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting P.sup.1 and X.sup.12 and/or P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then) X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined above for module A, wherein s=1, t=1, and u=1; X.sup.12 is Glyol; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or basic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or an alcoholic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one hydroxyl function; with the proviso that, if P.sup.1 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.m; is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or X.sup.12 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.10 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; the carbonyl (C═O) point of attachment of X.sup.12 and the nitrogen (N) point of attachment of X.sup.14 are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=1, t=1, and u=0; and P.sup.1 and X.sup.12 taken together and/or P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids or non-naturally cross-linking acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting P.sup.1 and X.sup.12 and/or P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; P.sup.11; and X.sup.12 are as defined above for module A, wherein s=1, t=1, and u=1; X.sup.13 is Glyol; or a naturally or non-naturally occurring aliphatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic amide function; with the proviso that, if P.sup.1 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; P.sup.m; or X.sup.12; is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.10 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; the carbonyl (C═O) point of attachment of X.sup.13 and the nitrogen (N) point of attachment of P.sup.1 are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A, wherein s=1, t=1, and u=1; P.sup.11 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; with the proviso that, if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.10; is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the carbonyl (C═O) point of attachment of P.sup.11 and the nitrogen (N) point of attachment of X.sup.14 are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=1, t=0, and u=0; and P.sup.1 and X.sup.12 taken together and/or P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids or non-naturally cross-linking acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting P.sup.1 and X.sup.12 and/or P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an alcoholic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined above for module A, wherein s=1, t=1, and u=1; X.sup.12 is Glyol; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic amide function; or an aliphatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a basic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or an alcoholic amino alcohol containing in total 1 to carbon- and/or heteroatoms in a single side-chain comprising at least one hydroxyl function; with the proviso that, if P.sup.1 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.m; is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or X.sup.12 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.10 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; the carbonyl (C═O) point of attachment of X.sup.12 and the nitrogen (N) point of attachment of P.sup.1 are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an alcoholic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A, wherein s=1, t=1, and u=1; P.sup.11 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; with the proviso that, if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.10; is a naturally or non-naturally occurring aromatic L a amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the carbonyl (C═O) point of attachment of P.sup.11 and the nitrogen (N) point of attachment of P′ are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; then P.sup.1 is a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an alcoholic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.2 is a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A, wherein s=1, t=1, and u=1; P.sup.11 is a naturally or non-naturally occurring aliphatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or guanidino function; or a naturally or non-naturally occurring alcoholic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; or a naturally or non-naturally occurring D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amide function; with the proviso that, if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.10; is a naturally or non-naturally occurring aromatic L a amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the nitrogen (N) point of attachment of P′ is appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acid optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; and a module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, and wherein Q.sup.1 is a naturally or non-naturally occurring basic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; Q.sup.2, Q.sup.5, and Q.sup.6 are independently a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; Q.sup.3 is a naturally or non-naturally occurring aliphatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; Q.sup.4 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; Q.sup.7 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and a linker L consisting of k=0-3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, and wherein, if k=1, L.sup.1 is Gly; Sar; Aib; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; if k=2, the additional element L.sup.2 is Gly; Sar; Aib; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; if k=3, the additional element L.sup.3 is Gly; Sar; Aib; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=1-3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the nitrogen (N) of 12; or, if k=0, then Q.sup.1 being directly connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the α-nitrogen (N) of Q.sup.1; or a tautomer or rotamer thereof; or a salt; or a pharmaceutically acceptable salt; or a hydrate; or a solvate thereof.

    2. Compounds of the formula (I) according to claim 1 comprising a module A consisting of single elements P or X being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element wherein s=0, t=0, and u=0; or s=1, t=0, and u=0; or s=0, t=0, and u=1; if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined for module A in claim 1, wherein s=1, t=1, and u=1; P.sup.11 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; with the proviso that, if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.m; is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the carbonyl (C═O) point of attachment of P.sup.11 and the nitrogen (N) point of attachment of X.sup.14 are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=1, t=0, and u=0; and P.sup.1 and X.sup.12 taken together and/or P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids or non-naturally cross-linking acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting P.sup.1 and X.sup.12 and/or P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an alcoholic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined for module A in claim 1, wherein s=1, t=1, and u=1; X.sup.12 is Glyol; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic amide function; or an aliphatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a basic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or one guanidino function; or an alcoholic amino alcohol containing in total 1 to carbon- and/or heteroatoms in a single side-chain comprising at least one hydroxyl function; with the proviso that, if P.sup.1 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.m; is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or X.sup.12 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic amino alcohol containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.10 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then X.sup.12 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; the carbonyl (C═O) point of attachment of X.sup.12 and the nitrogen (N) point of attachment of P.sup.1 are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together and/or P.sup.4 and P.sup.9 taken together form naturally or non-naturally cross-linking α-amino acids containing each in total 1 to 12 carbon- and/or heteroatoms in a single side-chain which together are connecting P.sup.2 and P.sup.11 and/or P.sup.4 and P.sup.9 by covalent interaction (interstrand linkage) or by electrostatic interaction (salt bridge); then P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an alcoholic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined for module A in claim 1, wherein s=1, t=1, and u=1; P.sup.11 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or guanidino function; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; with the proviso that, if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.m; is a naturally or non-naturally occurring aromatic L a amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the carbonyl (C═O) point of attachment of P.sup.11 and the nitrogen (N) point of attachment of P.sup.1 are appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acids optionally having modified carbonyl (C═O) functional groups and/or nitrogen (N) functional groups; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; then P.sup.1 is a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aromatic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an alcoholic L α-hydroxy acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or an aliphatic acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; P.sup.2 is a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined for module A in claim 1, wherein s=1, t=1, and u=1; P.sup.11 is a naturally or non-naturally occurring aliphatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function or guanidino function; or a naturally or non-naturally occurring alcoholic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxylic acid function or phosphonic acid function; or a naturally or non-naturally occurring D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amide function; with the proviso that, if P.sup.3 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.1; or P.sup.m; is a naturally or non-naturally occurring aromatic L α amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and if P.sup.8 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; then P.sup.10 is a naturally or non-naturally occurring aromatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the nitrogen (N) point of attachment of P′ is appropriately saturated to form the corresponding naturally or non-naturally occurring terminal α-amino acid optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is a naturally or non-naturally occurring α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one carboxyl function; and a module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, and wherein Q.sup.1 is a naturally or non-naturally occurring basic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; Q.sup.2, Q.sup.5, and Q.sup.6 are independently a naturally or non-naturally occurring basic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; Q.sup.3 is a naturally or non-naturally occurring aliphatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aromatic D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; Q.sup.4 is a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; Q.sup.7 is a naturally or non-naturally occurring alcoholic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring aliphatic L α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; and a linker L consisting of k=0-3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, and wherein, if k=1, L.sup.1 is Gly; Sar; Aib; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; if k=2, the additional element L.sup.2 is Gly; Sar; Aib; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; if k=3, the additional element L.sup.3 is Gly; Sar; Aib; or a naturally or non-naturally occurring aliphatic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; or a naturally or non-naturally occurring basic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain comprising at least one amino function; or a naturally or non-naturally occurring alcoholic L or D α-amino acid containing in total 1 to 25 carbon- and/or heteroatoms in a single side-chain; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=1-3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the nitrogen (N) of L.sup.1; or, if k=0, then Q.sup.1 being directly connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the α-nitrogen (N) of Q.sup.1; or a tautomer or rotamer thereof; or a salt; or a pharmaceutically acceptable salt; or a hydrate; or a solvate thereof.

    3. Compounds of the formula (I) according to any one of claim 1 or 2 comprising a module A consisting of single elements P or X being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, wherein if s=1, t=1, and u=1; and X.sup.14 and X.sup.13 taken together form an interstrand linking bis(amino acid)-structure of one of the formulae ##STR00452## based on the linkage of two α-amino acid residues; or an interstrand linking (amino acid)-(acid)-structure of one of the formulae ##STR00453## based on the linkage of an α-amino acid residue and an acid residue; or a salt bridge of one of the formulae ##STR00454## based on the electrostatic interaction between two α-amino acid residue as defined herein below; and/or P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid)-structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; X.sup.14 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or an α-amino acid residue of one of the formulae ##STR00455## or an acid residue of one of the formulae ##STR00456## P.sup.1 is an α-amino acid residue of one of the formulae ##STR00457## P.sup.2 is an L α-amino acid residue of one of the formulae ##STR00458## P.sup.3 is an L α-amino acid residue of one of the formulae ##STR00459## P.sup.4 is Gly; or an L α-amino acid residue of one of the formulae ##STR00460## P.sup.5 is Gly; or an L α-amino acid residue of formula ##STR00461## P.sup.6 is Gly; or a D α-amino acid residue of formula ##STR00462## P.sup.7 is Gly; or an α-amino acid residue of one of the formulae ##STR00463## P.sup.8 is an L α-amino acid residue of one of the formulae ##STR00464## P.sup.9 is Gly, or an L α-amino acid residue of one of the formulae ##STR00465## P.sup.10 is an L α-amino acid residue of one of the formulae ##STR00466## P.sup.11 is an L α-amino acid residue of one of the formulae ##STR00467## X.sup.12 is Gly; or an α-amino acid residue of one of the formulae ##STR00468## X.sup.13 is Glyol; or an α-amino acid residue of one of the formulae ##STR00469## with the proviso that, if P.sup.1 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; or AA1D; and if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; P.sup.m; or X.sup.12; is an α-amino acid residue of formula AA2; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and if P.sup.10 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; or AA1D; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the combined number of interstrand linkages and salt bridges in above module A must not exceed two; if X.sup.14 and X.sup.13 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.1 and X.sup.12 taken together are not forming an interstrand linkage or salt bridge, as defined above; if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or a salt bridge, as defined above; X.sup.13 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; X.sup.14 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with R.sup.1, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae ##STR00470## if s=1, t=0, and u=1; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; X.sup.12 is Glyol; or an L α-amino acid residue of one of the formulae ##STR00471## or an amino alcohol residue of one of the formulae ##STR00472## with the proviso that, if P.sup.1 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; and if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.10; is an α-amino acid residue of formula AA2; or X.sup.12 is an α-amino acid residue of formula AA2; or an amino alcohol residue of formula AA8; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and if P.sup.10 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; X.sup.12 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; X.sup.14 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with R.sup.1, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae ##STR00473## if s=1, t=1, and u=0; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or an interstrand linking (amino acid)-(acid)-structure of one of the formulae AA17; or AA17.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or an α-amino acid residue of one of the formulae ##STR00474## or an L α-hydroxy acid residue of one of the formulae ##STR00475## or an acid residue of one of the formulae ##STR00476## P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; P.sup.11; and X.sup.12 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; X.sup.13 is Glyol; or an α-amino acid residue of one of the formulae ##STR00477## with the proviso that, if P.sup.1 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; or AA1D; and if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; P.sup.m; or X.sup.12; is an α-amino acid residue of formula AA2; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and if P.sup.10 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; or AA1D; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; X.sup.13 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; P.sup.1 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with R.sup.1, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae ##STR00478## if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is an L α-amino acid residue of one of the formulae ##STR00479## with the proviso that, if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.m; is an α-amino acid residue of formula AA2; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, P.sup.11 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; X.sup.14 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with Fe, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae ##STR00480## if s=1, t=0, and u=0; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or an interstrand linking (amino acid)-(acid)-structure of one of the formulae AA17; or AA17.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or an α-amino acid residue of one of the formulae ##STR00481## or an L α-hydroxy acid residue of one of the formulae ##STR00482## or an acid residue of one of the formulae ##STR00483## P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; X.sup.12 is Glyol; or an α-amino acid residue of one of the formulae ##STR00484## or an amino alcohol residue of one of the formulae ##STR00485## with the proviso that, if P.sup.1 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; AA4; or AA4.sup.D; and if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.m; is an α-amino acid residue of formula AA2; or X.sup.12 is an α-amino acid residue of formula AA2; or an amino alcohol residue of formula AA8; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and if P.sup.10 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; X.sup.12 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; P.sup.1 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with Fe, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae ##STR00486## if s=0, t=0, and u=0; and alternatively P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19D; P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or an α-amino acid residue of one of the formulae ##STR00487## or an L α-hydroxy acid residue of one of the formulae ##STR00488## or an acid residue of one of the formulae ##STR00489## P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P8; P.sup.9; and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is an L α-amino acid residue of one of the formulae ##STR00490## with the proviso that, if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.10; is an α-amino acid residue of formula AA2; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, P.sup.11 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; P.sup.1 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with R.sup.1, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae ##STR00491## if s=0, t=0, and u=0; and P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; P.sup.1 is pGlu; or an α-amino acid residue of one of the formulae ##STR00492## or an L α-hydroxy acid residue of one of the formulae ##STR00493## or an acid residue of one of the formulae ##STR00494## P.sup.2 is an L α-amino acid residue of formula ##STR00495## P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P8; P.sup.9; and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is an α-amino acid residue of one of the formulae ##STR00496## with the proviso that, if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.m; is an α-amino acid residue of formula AA2; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, P.sup.1 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with Fe, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae ##STR00497## and a module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, and wherein Q.sup.1 is an α-amino acid residue of one of the formulae ##STR00498## Q.sup.2, Q.sup.5, and Q.sup.6 are independently an L α-amino acid residue of formula ##STR00499## Q.sup.3 is a D α-amino acid residue of one of the formulae ##STR00500## Q.sup.4 is an L α-amino acid residue of one of the formulae ##STR00501## Q.sup.7 is an L α-amino acid residue of one of the formulae ##STR00502## and a linker L consisting of k=0-3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, and wherein, if k=1, L.sup.1 is Gly; Sar; Aib; or an α-amino acid residue of one of the formulae AA3b; AA3b.sup.D; AA4; AA4.sup.D; AA1; or AA1.sup.D, as depicted above; if k=2, the additional element L.sup.2 is Gly; Sar; Aib; or an α-amino acid residue of one of the formulae AA3b; AA3b.sup.D; AA4; AA4.sup.D; AA1; or AA1.sup.D, as depicted above; if k=3, the additional element L.sup.3 is Gly; Sar; Aib; or an α-amino acid residue of one of the formulae AA3b; AA3b.sup.D; AA4; AA4.sup.D; AA1; or AA1.sup.D, as depicted above; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=1-3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the nitrogen (N) of L.sup.1; or, if k=0, then Q.sup.1 being directly connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the α-nitrogen (N) of Q.sup.1; R.sup.Alk is, with the proviso of containing less than 26 carbon- and/or heteroatoms, C.sub.1-12-alkyl; C.sub.2-12-alkenyl; cycloalkyl; cycloalkyl-C.sub.1-6-alkyl; or C.sub.1-6-alkoxy-C.sub.1-6-alkyl; R.sup.Ar is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.4).sub.nR.sup.19; —(CH.sub.2).sub.nO(CH.sub.2).sub.mR.sup.19; —(CH.sub.2).sub.nS(CH.sub.2).sub.mR.sup.19; or —(CH.sub.2).sub.nNR.sup.14(CH.sub.2).sub.mR.sup.19; R.sup.Arn1 is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qNR.sup.15R.sup.16; —(CH.sub.2).sub.qC(═NR.sup.13)NR.sup.15R.sup.16; —(CH.sub.2).sub.qC(═NNR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CR.sup.1R.sup.13).sub.qNR.sup.2C(═NR.sup.17)NR.sup.15R.sup.16; —(CR.sup.1R.sup.13).sub.qN═C(NR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CH.sub.2).sub.nO(CH.sub.2).sub.mNR.sup.15R.sup.16; —(CH.sub.2).sub.nO(CH.sub.2).sub.mC(═NR.sup.17)NR.sup.15R.sup.16; —(CH.sub.2).sub.nO(CH.sub.2).sub.mC(═NNR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CH.sub.2).sub.nO(CH.sub.2).sub.nNR.sup.1C(═NR.sup.17)NR.sup.15R.sup.16; —(CH.sub.2).sub.nO(CH.sub.2).sub.nN═C(NR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CH.sub.2).sub.nS(CH.sub.2).sub.mNR.sup.15R.sup.16; —(CH.sub.2).sub.nS(CH.sub.2).sub.mC(═NR.sup.17)NR.sup.15R.sup.16; —(CH.sub.2).sub.nS(CH.sub.2).sub.mC(═NNR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CH.sub.2).sub.nS(CH.sub.2).sub.mNR.sup.1C(═NR.sup.17)NR.sup.15R.sup.16; —(CH.sub.2).sub.nS(CH.sub.2).sub.mN═C(NR.sup.15R.sup.16)NR.sup.17R.sup.18; or —(CR.sup.1R.sup.13).sub.qNR.sup.14R.sup.27; R.sup.Am2 is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qNR.sup.15R.sup.16; —(CH.sub.2).sub.nO(CH.sub.2).sub.mNR.sup.15R.sup.16; or —(CH.sub.2).sub.nS(CH.sub.2).sub.mNR.sup.15R.sup.16 R.sup.Acid is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qCOOH; or —(CR.sup.1R.sup.13).sub.q PO(OH).sub.2; R.sup.OH is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qOH; —(CR.sup.1R.sup.13).sub.qSH; —(CH.sub.2).sub.nO(CH.sub.2).sub.mOH; —(CH.sub.2).sub.nS(CH.sub.2).sub.mOH; —(CH.sub.2).sub.nNR.sup.1(CH.sub.2).sub.mOH; hydroxy-C.sub.1-8-alkyl; hydroxy-C.sub.2-8-alkenyl; hydroxy-cycloalkyl; or hydroxy-heterocycloalkyl; R.sup.Amide is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qCONR.sup.15R.sup.16; Y is, with the proviso of containing less than 25 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.q—; Z is, with the proviso of containing less than 25 carbon- and/or heteroatoms, —(CH.sub.2).sub.n—S—S—(CH.sub.2).sub.m—; —(CR.sup.28R.sup.29).sub.n—S—S—(CR.sup.28R.sup.29).sub.m—; —(CH.sub.2).sub.nCH═CH(CH.sub.2).sub.m—; —(CR.sup.28R.sup.29).sub.nCH═CH(CR.sup.28R.sup.29).sub.m—; —(CH.sub.2).sub.n-heteroaryl-(CH.sub.2).sub.m—; —(CR.sup.28R.sup.29).sub.n-heteroaryl-(CR.sup.28R.sup.29).sub.m—; —(CH.sub.2).sub.nCONR.sup.1(CH.sub.2).sub.m—; —(CH.sub.2).sub.nNR.sup.1CO(CH.sub.2).sub.m— —(CR.sup.28R.sup.29).sub.nCONR.sup.1(CR.sup.28R.sup.29).sub.m—; —(CR.sup.28R.sup.29)NR.sup.1CO(CR.sup.28R.sup.29).sub.m—; —(CH.sub.2).sub.nNR.sup.1CONR.sup.2(CH.sub.2).sub.m—; or —(CR.sup.28R.sup.29).sub.nNR.sup.1CONR.sup.2(CR.sup.28R.sup.29).sub.m—; R.sup.1 and R.sup.2 are independently H; CF.sub.3; C.sub.1-8-alkyl; or C.sub.2-8-alkenyl; R.sup.4 is H; F; CF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; cycloalkyl; heterocycloalkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; —(CHR.sup.13).sub.oOR.sup.15; —O(CO)R.sup.15; —(CHR.sup.13).sub.oSR.sup.15; —(CHR.sup.13).sub.oNR.sup.15R.sup.16; —(CHR.sup.13).sub.oOCONR.sup.15R.sup.16; —(CHR.sup.13).sub.oNR.sup.1CONR.sup.15R.sup.16; —(CHR.sup.13).sub.oNR.sup.1COR.sup.15; —(CHR.sup.13).sub.oCOOR.sup.15; —(CHR.sup.13).sub.oCONR.sup.15R.sup.16; —(CHR.sup.13).sub.oPO(OR.sup.1).sub.2; —(CHR.sup.13).sub.oSO.sub.2R.sup.15; —(CHR.sup.13).sub.oNR.sup.1SO.sub.2R.sup.15; —(CHR.sup.13).sub.oSO.sub.2NR.sup.15R.sup.16; —(CR.sup.1R.sup.13).sub.oR.sup.19; or —(CHR.sup.1).sub.nO(CHR.sup.2).sub.mR.sup.23; or R.sup.13 is H; F; CF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; cycloalkyl; heterocycloalkyl; cycloalkyl-C.sub.1-6-alkyl; heterocycloalkyl-C.sub.1-6-alkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; —(CHR.sup.1).sub.oOR.sup.15; —OCOR.sup.1; —(CHR.sup.1).sub.oNR.sup.15R.sup.16; CHR.sup.1OR.sup.2C(═NR.sup.17)NR.sup.15R.sup.16; —(CHR.sup.1OR.sup.2CONR.sup.15R.sup.16; —COOR.sup.15; —CONR.sup.15R.sup.16; or —SO.sub.2R.sup.15; or —SO.sub.2NR.sup.15R.sup.16; R.sup.14 is H; CF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; cycloalkyl; heterocycloalkyl; cycloalkyl-C.sub.1-6-alkyl; heterocycloalkyl-C.sub.1-6-alkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; cycloalkyl-aryl; heterocycloalkyl-aryl; cycloalkyl-heteroaryl; heterocycloalkyl-heteroaryl; aryl-cycloalkyl; aryl-heterocycloalkyl; heteroaryl-cycloalkyl; heteroaryl-heterocycloalkyl; —(CHR.sup.1).sub.oOR.sup.15; —(CHR.sup.1).sub.oSR.sup.15; —(CHR.sup.1).sub.oNR.sup.15R.sup.16; —(CHR.sup.1).sub.oCOOR.sup.15; —(CHR.sup.1).sub.oCONR.sup.15R.sup.16; or —(CHR.sup.1).sub.oSO.sub.2R.sup.15; R.sup.15, R.sup.16, R.sup.17 and R.sup.18 are independently H; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; C.sub.1-6-alkoxy; cycloalkyl; heterocycloalkyl; cycloalkyl-C.sub.1-6-alkyl; heterocycloalkyl-C.sub.1-6-alkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; cycloalkyl-aryl; heterocycloalkyl-aryl; cycloalkyl-heteroaryl; heterocycloalkyl-heteroaryl; aryl-cycloalkyl; aryl-heterocycloalkyl; heteroaryl-cycloalkyl; or heteroaryl-heterocycloalkyl; or the structural elements —NR.sup.15R.sup.16 and —NR.sup.17R.sup.18 can independently form: heterocycloalkyl; aryl-heterocycloalkyl; or heteroaryl-heterocycloalkyl; R.sup.19 is an aryl group of one of the formulae ##STR00503## or a group of one of the formulae ##STR00504## ##STR00505## X, X′, X″ and X′″ are independently —CR.sup.20; or N; R.sup.20 and R.sup.21 are independently H; F; Cl; Br; I; OH; NH.sub.2; NO.sub.2; CN; CF.sub.3; OCHF.sub.2; OCF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; —(CH.sub.2).sub.oR.sup.22; —(CH.sub.2).sub.oOR.sup.15; —O(CO)R.sup.15; —O(CH.sub.2).sub.oR.sup.22; —(CH.sub.2).sub.oSR.sup.15; —(CH.sub.2).sub.oNR.sup.15R.sup.16; —(CH.sub.2).sub.oOCONR.sup.15R.sup.16; —(CH.sub.2).sub.oNR.sup.1CONR.sup.15R.sup.16; —(CH.sub.2).sub.oNR.sup.1COR.sup.15; —(CH.sub.2).sub.oCOOR.sup.15; —(CH.sub.2).sub.oCONR.sup.15R.sup.16; —(CH.sub.2).sub.oPO(OR.sup.1).sub.2; —(CH.sub.2).sub.oSO.sub.2R.sup.15; or —(CH.sub.2).sub.oOCOR.sup.15; R.sup.22 is an aryl group of the formula ##STR00506## R.sup.23, R.sup.24 and R.sup.25 are independently H; F; Cl; Br; I; OH; NH.sub.2; NO.sub.2; CN; CF.sub.3; OCHF.sub.2; OCF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; —(CH.sub.2).sub.oOR.sup.15; —O(CO)R.sup.15; —(CH.sub.2).sub.oNR.sup.1R.sup.15; —(CH.sub.2).sub.oCOOR.sup.15; —(CH.sub.2).sub.oCONR.sup.1R.sup.15; R.sup.26 is H; Ac; C.sub.1-8-alkyl; or aryl-C.sub.1-6-alkyl; R.sup.27 is —CO(CR.sup.1R.sup.13).sub.qR.sup.15; R.sup.28 and R.sup.29 are independently H; CF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; or aryl-C.sub.1-6-alkyl; cycloalkyl-C.sub.1-6-alkyl; or heterocycloalkyl-C.sub.1-6-alkyl; R.sup.30 is —OR.sup.14; —SR.sup.14; or —NR.sup.15R.sup.16; R.sup.31 is H; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; C.sub.1-6-alkoxy; cycloalkyl; heterocycloalkyl; cycloalkyl-C.sub.1-6-alkyl; heterocycloalkyl-C.sub.1-6-alkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; cycloalkyl-aryl; heterocycloalkyl-aryl; cycloalkyl-heteroaryl; heterocycloalkyl-heteroaryl; aryl-cycloalkyl; aryl-heterocycloalkyl; heteroaryl-cycloalkyl; heteroaryl-heterocycloalkyl; —COR.sup.15; —CONR.sup.15R.sup.16; —C(═NR.sup.13)NR.sup.15R.sup.16; or the structural element —NR.sup.1R.sup.31 can form: —N═C(NR.sup.15R.sup.16).sub.2; heterocycloalkyl; aryl-heterocycloalkyl; or heteroaryl-heterocycloalkyl; n and m are independently an integer of 0-5 with the proviso that n+m≤6; o is 0-4; p is 2-6; q is 1-6; and r is 1-3; or a tautomer or rotamer thereof; or a salt; or a pharmaceutically acceptable salt; or a hydrate; or a solvate thereof.

    4. Compounds of the formula (I) according to any one of claims 1 to 3 comprising a module A consisting of single elements P or X being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, wherein s=0, t=0, and u=0; or s=1, t=0, and u=0; or s=0, t=0, and u=1; if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P8; P.sup.9; and P.sup.10 are as defined for module A in claim 3, wherein s=1, t=1, and u=1; P.sup.11 is an L α-amino acid residue of one of the formulae AA1; AA3b; AA4; or AA5; with the proviso that, if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.m; is an α-amino acid residue of formula AA2; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, P.sup.11 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; X.sup.14 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with R.sup.1, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae AA20; or AA20.sup.D; if s=1, t=0, and u=0; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or an interstrand linking (amino acid)-(acid)-structure of one of the formulae AA17; or AA17.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or an α-amino acid residue of one of the formulae AA1; AA1.sup.D; AA2; or AA4; or an L α-hydroxy acid residue of one of the formulae AA11; AA12; or AA14; or an acid residue of one of the formulae AA15a; or AA15b; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P8; P.sup.9; P.sup.10; and P.sup.11 are as defined for module A in claim 3, wherein s=1, t=1, and u=1; X.sup.12 is Glyol; or an α-amino acid residue of one of the formulae AA1; AA2; AA3; AA4; AA4.sup.D; or AA6; or an amino alcohol residue of one of the formulae AA7; AA8; AA9; or AA10; with the proviso that, if P.sup.1 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; AA4; or AA4.sup.D; and if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.m; is an α-amino acid residue of formula AA2; or X.sup.12 is an α-amino acid residue of formula AA2; or an amino alcohol residue of formula AA8; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and if P.sup.10 is an α-amino acid residue of formula AA4; then X.sup.12 is an α-amino acid residue of formula AA1; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; X.sup.12 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; P.sup.1 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with Fe, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae AA20; or AA20.sup.1); if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure of one of the formulae AA16; or AA16.sup.D; or a salt bridge of one of the formulae AA18; AA18.sup.D; AA19; or AA19.sup.D; P.sup.1 is pGlu; .sup.DpGlu; Ac-pGlu; Ac-.sup.DpGlu; or an α-amino acid residue of one of the formulae AA1; AA1.sup.D; AA2; or AA4; or an L α-hydroxy acid residue of one of the formulae AA11; AA12; or AA14; or an acid residue of one of the formulae AA15a; or AA15b; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P8; P.sup.9; and P.sup.10 are as defined for module A in claim 3, wherein s=1, t=1, and u=1; P.sup.11 is an L α-amino acid residue of one of the formulae AA1; AA3b; AA4; or AA5; with the proviso that, if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.m; is an α-amino acid residue of formula AA2; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, P.sup.11 having a carbonyl (C═O) point of attachment not connected as aforementioned, being appropriately saturated by linkage with R.sup.30 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified carbonyl (C═O) functional group; P.sup.1 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with R.sup.1, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae AA20; or AA20.sup.D; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; P.sup.1 is pGlu; or an α-amino acid residue of one of the formulae AA1; AA1.sup.D; AA2; or AA4; or an L α-hydroxy acid residue of one of the formulae AA11; AA12; or AA14; or an acid residue of one of the formulae AA15a; or AA15b; P.sup.2 is an L α-amino acid residue of formula AA3b; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P8; P.sup.9; and P.sup.10 are as defined for module A in claim 3, wherein s=1, t=1, and u=1; P.sup.11 is an D α-amino acid residue of one of the formulae AA1.sup.D; AA2.sup.D; AA3b.sup.D; AA4.sup.D; AA5.sup.D; or AA6.sup.D; with the proviso that, if P.sup.3 is an α-amino acid residue of one of the formulae AA1; or AA4; then P.sup.1; or P.sup.m; is an α-amino acid residue of formula AA2; and if P.sup.8 is an α-amino acid residue of formula AA1; then P.sup.10 is an α-amino acid residue of formula AA2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, P.sup.1 having a nitrogen (N) not connected as aforementioned, being appropriately saturated by linkages with R.sup.1, as already depicted above, and R.sup.31 to form the corresponding naturally or non-naturally occurring terminal α-amino acid residue; optionally having a modified nitrogen (N) functional group; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is an α-amino acid residue of one of the formulae AA20; or AA20.sup.D; and a module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, and wherein Q.sup.1 is an α-amino acid residue of one of the formulae AA21; or AA21.sup.D; Q.sup.2, Q.sup.5, and Q.sup.6 are independently an L α-amino acid residue of formula AA3b; Q.sup.3 is a D α-amino acid residue of one of the formulae AA1.sup.D; or AA2.sup.D; Q.sup.4 is an L α-amino acid residue of one of the formulae AA1; or AA4; Q.sup.7 is an L α-amino acid residue of one of the formulae AA1; or AA4; and a linker L consisting of k=0-3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, and wherein, if k=1, L.sup.1 is Gly; Sar; Aib; or an α-amino acid residue of one of the formulae AA3b; AA3b.sup.D; AA4; AA4.sup.D; AA1; or AA1.sup.D, as depicted above; if k=2, the additional element L.sup.2 is Gly; Sar; Aib; or an α-amino acid residue of one of the formulae AA3b; AA3b.sup.D; AA4; AA4.sup.D; AA1; or AA1.sup.D, as depicted above; if k=3, the additional element L.sup.3 is Gly; Sar; Aib; or an α-amino acid residue of one of the formulae AA3b; AA3b.sup.D; AA4; AA4.sup.D; AA1; or AA1.sup.D, as depicted above; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=1-3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the nitrogen (N) of L.sup.1; or, if k=0, then Q.sup.1 being directly connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the α-nitrogen (N) of Q.sup.1; R.sup.Alk is, with the proviso of containing less than 26 carbon- and/or heteroatoms, C.sub.1-12-alkyl; C.sub.2-12-alkenyl; cycloalkyl; cycloalkyl-C.sub.1-6-alkyl; or C.sub.1-6-alkoxy-C.sub.1-6-alkyl; R.sup.Ar is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.4).sub.nR.sup.19; —(CH.sub.2).sub.nO(CH.sub.2).sub.mR.sup.19; —(CH.sub.2).sub.nS(CH.sub.2).sub.mR.sup.19; or —(CH.sub.2).sub.nNR.sup.14(CH.sub.2).sub.mR.sup.19; R.sup.Arn1 is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qNR.sup.15R.sup.16; —(CH.sub.2).sub.qC(═NR.sup.13)NR.sup.15R.sup.16; —(CH.sub.2).sub.qC(═NNR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CR.sup.1R.sup.13).sub.qNR.sup.2C(═NR.sup.17)NR.sup.15R.sup.16; —(CR.sup.1R.sup.13).sub.qN═C(NR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CH.sub.2).sub.nO(CH.sub.2).sub.mNR.sup.15R.sup.16; —(CH.sub.2).sub.nO(CH.sub.2).sub.mC(═NR.sup.17)NR.sup.15R.sup.16; —(CH.sub.2).sub.nO(CH.sub.2).sub.mC(═NNR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CH.sub.2).sub.nO(CH.sub.2).sub.nNR.sup.1C(═NR.sup.17)NR.sup.15R.sup.16; —(CH.sub.2).sub.nO(CH.sub.2).sub.nN═C(NR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CH.sub.2).sub.nS(CH.sub.2).sub.mNR.sup.15R.sup.16; —(CH.sub.2).sub.nS(CH.sub.2).sub.mC(═NR.sup.17)NR.sup.15R.sup.16; —(CH.sub.2).sub.nS(CH.sub.2).sub.mC(═NNR.sup.15R.sup.16)NR.sup.17R.sup.18; —(CH.sub.2).sub.nS(CH.sub.2).sub.mNR.sup.1C(═NR.sup.17)NR.sup.15R.sup.16; —(CH.sub.2).sub.nS(CH.sub.2).sub.mN═C(NR.sup.15R.sup.16)NR.sup.17R.sup.18; or —(CR.sup.1R.sup.13).sub.qNR.sup.14R.sup.27; R.sup.Arn2 is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qNR.sup.15R.sup.16; —(CH.sub.2).sub.nO(CH.sub.2).sub.mNR.sup.15R.sup.16; or —(CH.sub.2).sub.nS(CH.sub.2).sub.mNR.sup.15R.sup.16 R.sup.Acid is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qCOOH; or —(CR.sup.1R.sup.13).sub.q PO(OH).sub.2; R.sup.OH is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qOH; —(CR.sup.1R.sup.13).sub.qSH; —(CH.sub.2).sub.nO(CH.sub.2).sub.mOH; —(CH.sub.2).sub.nS(CH.sub.2).sub.mOH; —(CH.sub.2).sub.nNR.sup.1(CH.sub.2).sub.mOH; hydroxy-C.sub.1-8-alkyl; hydroxy-C.sub.2-8-alkenyl; hydroxy-cycloalkyl; or hydroxy-heterocycloalkyl; R.sup.Amide is, with the proviso of containing less than 26 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.qCONR.sup.15R.sup.16; Y is, with the proviso of containing less than 25 carbon- and/or heteroatoms, —(CR.sup.1R.sup.13).sub.q—; Z is, with the proviso of containing less than 25 carbon- and/or heteroatoms, —(CH.sub.2).sub.n—S—S—(CH.sub.2).sub.m—; —(CR.sup.28R.sup.29).sub.n—S—S—(CR.sup.28R.sup.29).sub.m—; —(CH.sub.2).sub.nCH═CH(CH.sub.2).sub.m—; —(CR.sup.28R.sup.29).sub.nCH═CH(CR.sup.28R.sup.29).sub.m—; —(CH.sub.2).sub.n-heteroaryl-(CH.sub.2).sub.m—; —(CR.sup.28R.sup.29).sub.n-heteroaryl-(CR.sup.28R.sup.29).sub.m—; —(CH.sub.2).sub.nCONR.sup.1(CH.sub.2).sub.m—; —(CH.sub.2).sub.nNR.sup.1CO(CH.sub.2).sub.m— —(CR.sup.28R.sup.29).sub.nCONR.sup.1(CR.sup.28R.sup.29).sub.m—; —(CR.sup.28R.sup.29)NR.sup.1CO(CR.sup.28R.sup.29).sub.m—; —(CH.sub.2).sub.nNR.sup.1CONR.sup.2(CH.sub.2).sub.m—; or —(CR.sup.28R.sup.29).sub.nNR.sup.1CONR.sup.2(CR.sup.28R.sup.29).sub.m—; R.sup.1 and R.sup.2 are independently H; CF.sub.3; C.sub.1-8-alkyl; or C.sub.2-8-alkenyl; R.sup.4 is H; F; CF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; cycloalkyl; heterocycloalkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; —(CHR.sup.13).sub.oOR.sup.15; —O(CO)R.sup.15; —(CHR.sup.13).sub.oSR.sup.15; —(CHR.sup.13).sub.oNR.sup.15R.sup.16; —(CHR.sup.13).sub.oOCONR.sup.15R.sup.16; —(CHR.sup.13).sub.oNR.sup.1CONR.sup.15R.sup.16; —(CHR.sup.13).sub.oNR.sup.1COR.sup.15; —(CHR.sup.13).sub.oCOOR.sup.15; —(CHR.sup.13).sub.oCONR.sup.15R.sup.16; —(CHR.sup.13).sub.oPO(OR.sup.1).sub.2; —(CHR.sup.13).sub.oSO.sub.2R.sup.15; —(CHR.sup.13).sub.oNR.sup.1SO.sub.2R.sup.15; —(CHR.sup.13).sub.oSO.sub.2NR.sup.15R.sup.16; —(CR.sup.1R.sup.13).sub.oR.sup.19; or —(CHR.sup.1).sub.nO(CHR.sup.2).sub.mR.sup.23; or R.sup.13 is H; F; CF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; cycloalkyl; heterocycloalkyl; cycloalkyl-C.sub.1-6-alkyl; heterocycloalkyl-C.sub.1-6-alkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; —(CHR.sup.1).sub.oOR.sup.15; —OCOR.sup.1; —(CHR.sup.1).sub.oNR.sup.15R.sup.16; CHR.sup.1OR.sup.2C(═NR.sup.17)NR.sup.15R.sup.16; —(CHR.sup.1OR.sup.2CONR.sup.15R.sup.16; —COOR.sup.15; —CONR.sup.15R.sup.16; or —SO.sub.2R.sup.15; or —SO.sub.2NR.sup.15R.sup.16; R.sup.14 is H; CF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; cycloalkyl; heterocycloalkyl; cycloalkyl-C.sub.1-6-alkyl; heterocycloalkyl-C.sub.1-6-alkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; cycloalkyl-aryl; heterocycloalkyl-aryl; cycloalkyl-heteroaryl; heterocycloalkyl-heteroaryl; aryl-cycloalkyl; aryl-heterocycloalkyl; heteroaryl-cycloalkyl; heteroaryl-heterocycloalkyl; —(CHR.sup.1).sub.oOR.sup.15; —(CHR.sup.1).sub.oSR.sup.15; —(CHR.sup.1).sub.oNR.sup.15R.sup.16; —(CHR.sup.1).sub.oCOOR.sup.15; —(CHR.sup.1).sub.oCONR.sup.15R.sup.16; or —(CHR.sup.1).sub.oSO.sub.2R.sup.15; R.sup.15, R.sup.16, R.sup.17 and R.sup.18 are independently H; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; C.sub.1-6-alkoxy; cycloalkyl; heterocycloalkyl; cycloalkyl-C.sub.1-6-alkyl; heterocycloalkyl-C.sub.1-6-alkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; cycloalkyl-aryl; heterocycloalkyl-aryl; cycloalkyl-heteroaryl; heterocycloalkyl-heteroaryl; aryl-cycloalkyl; aryl-heterocycloalkyl; heteroaryl-cycloalkyl; or heteroaryl-heterocycloalkyl; or the structural elements —NR.sup.15R.sup.16 and —NR.sup.17R.sup.18 can independently form: heterocycloalkyl; aryl-heterocycloalkyl; or heteroaryl-heterocycloalkyl; R.sup.19 is an aryl group of one of the formulae ##STR00507## or a group of one of the formulae ##STR00508## ##STR00509## X, X′, X″ and X′″ are independently —CR.sup.20; or N; R.sup.20 and R.sup.21 are independently H; F; Cl; Br; I; OH; NH.sub.2; NO.sub.2; CN; CF.sub.3; OCHF.sub.2; OCF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; —(CH.sub.2).sub.oR.sup.22; —(CH.sub.2).sub.oOR.sup.15; —O(CO)R.sup.15; —O(CH.sub.2).sub.oR.sup.22; —(CH.sub.2).sub.oSR.sup.15; —(CH.sub.2).sub.oNR.sup.15R.sup.16; —(CH.sub.2).sub.oOCONR.sup.15R.sup.16; —(CH.sub.2).sub.oNR.sup.1CONR.sup.15R.sup.16; —(CH.sub.2).sub.oNR.sup.1COR.sup.15; —(CH.sub.2).sub.oCOOR.sup.15; —(CH.sub.2).sub.oCONR.sup.15R.sup.16; —(CH.sub.2).sub.oPO(OR.sup.1).sub.2; —(CH.sub.2).sub.oSO.sub.2R.sup.15; or —(CH.sub.2).sub.oCOR.sup.15; R.sup.22 is an aryl group of the formula ##STR00510## R.sup.23, R.sup.24 and R.sup.25 are independently H; F; Cl; Br; I; OH; NH.sub.2; NO.sub.2; CN; CF.sub.3; OCHF.sub.2; OCF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; —(CH.sub.2).sub.oOR.sup.15; —O(CO)R.sup.15; —(CH.sub.2).sub.oNR.sup.1R.sup.15; —(CH.sub.2).sub.oCOOR.sup.15; —(CH.sub.2).sub.oCONR.sup.1R.sup.15; R.sup.26 is H; Ac; C.sub.1-8-alkyl; or aryl-C.sub.1-6-alkyl; R.sup.27 is —CO(CR.sup.1R.sup.13).sub.qR.sup.15; R.sup.28 and R.sup.29 are independently H; CF.sub.3; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; or aryl-C.sub.1-6-alkyl; cycloalkyl-C.sub.1-6-alkyl; or heterocycloalkyl-C.sub.1-6-alkyl; R.sup.30 is —OR.sup.14; —SR.sup.14; or —NR.sup.15R.sup.16; R.sup.31 is H; C.sub.1-8-alkyl; C.sub.2-8-alkenyl; C.sub.1-6-alkoxy; cycloalkyl; heterocycloalkyl; cycloalkyl-C.sub.1-6-alkyl; heterocycloalkyl-C.sub.1-6-alkyl; aryl; heteroaryl; aryl-C.sub.1-6-alkyl; heteroaryl-C.sub.1-6-alkyl; cycloalkyl-aryl; heterocycloalkyl-aryl; cycloalkyl-heteroaryl; heterocycloalkyl-heteroaryl; aryl-cycloalkyl; aryl-heterocycloalkyl; heteroaryl-cycloalkyl; heteroaryl-heterocycloalkyl; —COR.sup.15; —CONR.sup.15R.sup.16; —C(═NR.sup.13)NR.sup.15R.sup.16; or the structural element —NR.sup.1R.sup.31 can form: —N═C(NR.sup.15R.sup.16).sup.2; heterocycloalkyl; aryl-heterocycloalkyl; or heteroaryl-heterocycloalkyl; n and m are independently an integer of 0-5 with the proviso that n+m 6; o is 0-4; p is 2-6; q is 1-6; and r is 1-3; or a tautomer or rotamer thereof; or a salt; or a pharmaceutically acceptable salt; or a hydrate; or a solvate thereof.

    5. Compounds according to any one of claims 1 to 4 wherein specifically for module A, if s=1, t=1, and u=1; and X.sup.14 and X.sup.13 taken together form an interstrand linking bis(amino acid)-structure or (amino acid)-(acid) structure based on the linkage of two L amino acid residues; or an amino acid residue and an acid residue; following connection of the side chain of Cys; Pen; Hcy; Ac-Cys; Ac-Pen; Ac-Hcy; or 3MPA with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hey-NH.sub.2; by a disulfide linkage; or connection of the side chain of Ac-Dab; Ac-Dap; Dab; or Dap; at X.sup.14 with the side chain of Glu-NH.sub.2; Asp-NH.sub.2; Glu; or Asp; at X.sup.13; or the side chain of Ac-Glu; Ac-Asp; Glu; or Asp; at X.sup.14 with the side chain of Dab-NH.sub.2; Dap-NH.sub.2; Dab; or Dap; at X.sup.13; by a lactam linkage; or X.sup.14 and X.sup.13 taken together form a salt bridge based on the electrostatic interaction between the side chain of Ac-Dab; Ac-Dap; Ac-Lys; Dab; Dap; or Lys; at X.sup.14 and the side chain of Glu-NH.sub.2; Asp-NH.sub.2; Glu; or Asp; at X.sup.13; or the side chain of Ac-Glu; Ac-Asp; Glu; or Asp; at X.sup.14 and the side chain of Dab-NH.sub.2; Dap-NH.sub.2; Lys-NH.sub.2; Dab; Dap; or Lys; at X.sup.13; and/or P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; at P.sup.2 with the side chain of Glu; or Asp; at P.sup.11; or the side chain Glu; or Asp; at P.sup.2 with the side chain of Dab; or Dap; at P.sup.11; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; X.sup.14 is .sup.DSer; pGlu; .sup.DpGlu; Ac-Dab; Dab; 6MeHeptA; Ac-pGlu; Ac-.sup.DpGlu; or Ac-.sup.DSer; P.sup.1 is Val; NMeVal; .sup.DVal; Leu; Ile; Nle; Phe; Tyr; Ser; Leu(3R)OH; or Nva; P.sup.2 is Thr; Dap; Ala; Val tBuGly; or Dab; P.sup.3 is Tyr; Val; Ser; or Thr; P.sup.4 is Dab; Dap; Ser; His; or Gly; P.sup.5 is Gly; Ala; Val; Abu; His; Thr; or Orn; P.sup.6 is .sup.DDab; .sup.DArg; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Hse; Thr; Dab; Dap; Ala; or Gly; P.sup.8 is Trp; or Val; P.sup.9 is Ser; Hse; Thr; alloThr; Dab; His; Glu; Ala; or Gly; P.sup.10 is Val; tBuGly; Tyr; Trp; Ser; Nva; or Ile; P.sup.11 is Ala; Ser; Thr; Dab; or Glu; X.sup.12 is Val; Ser; Thr; Dab; .sup.DAla; Gly; or Tyr; X.sup.13 is .sup.DAla; .sup.DAla-NH.sub.2; .sup.DSer; .sup.DSer-NH.sub.2; or Glyol; with the proviso that, if P.sup.1 is Ser; or Leu(3R)OH; then X.sup.12 is Val; or .sup.DAla; and if P.sup.3 is Ser; Thr; or Val; then P.sup.1; P.sup.10; or X.sup.12; is Tyr; and if P.sup.8 is Val; then P.sup.10 is Trp; and if P.sup.10 is Ser; then X.sup.12 is Val; or .sup.DAla; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, the combined number of interstrand linkages and salt bridges in above module A must not exceed two; if X.sup.14 and X.sup.13 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.1 and X.sup.12 taken together are not forming an interstrand linkage or salt bridge, as defined above; if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or a salt bridge, as defined above; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=1, t=0, and u=1; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hey-NH.sub.2 by a disulfide linkage; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; with the side chain of Glu; or Asp; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; X.sup.12 is Val; Ser; Thr; Dab; Tyr; Serol; Throl; .sup.DThrol; Tyrol; Glyol; Val-NH.sub.2; Ser-NH.sub.2; Ser-NHMe; Ser-OiPr; Thr-NH.sub.2; Dab-NH.sub.2; Tyr-NH.sub.2; with the proviso that, if P.sup.1 is Ser; or Leu(3R)OH; then X.sup.12 is Val; or Val-NH.sub.2; and if P.sup.3 is Ser; Thr; or Val; then P.sup.1; or P.sup.m; is Tyr; or X.sup.12 is Tyr; Tyrol; or Tyr-NH.sub.2; and if P.sup.8 is Val; then P.sup.10 is Trp; and if P.sup.10 is Ser; then X.sup.12 is Val; or Val-NH.sub.2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=1, t=1, and u=0; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; Hcy; Ac-Cys; Ac-Pen; or Ac-Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; with the side chain of Glu; or Asp; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; P.sup.1 is Val; NMeVal; .sup.DVal; Leu; Ile; Nle; Phe; Tyr; Ser; Leu(3R)OH; Nva; HOVal; Ac-Val; Ac-.sup.DVal; Ac-Leu; Ac-Ile; Ac-Phe; Prop-Val; Ac-Nle; Ac-Tyr; Ac-Ser; Ac-Leu(3R)OH; Ac-Nva; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 and X.sup.12 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; X.sup.13 is .sup.DAla; .sup.DAla-NH.sub.2; .sup.DSer; .sup.DSer-N H.sub.2; .sup.DThr; .sup.DAsp; Ser; Asp; Asn; or Glyol; with the proviso that, if P.sup.1 is Ser; Ac-Ser; Leu(3R)OH; or Ac-Leu(3R)OH; then X.sup.12 is Val; and if P.sup.3 is Ser; Thr; or Val; then P.sup.1; is Tyr; or Ac-Tyr; or P.sup.10; or X.sup.12; is Tyr; and if P.sup.8 is Val; then P.sup.10 is Trp; and if P.sup.10 is Ser; then X.sup.12 is Val; or .sup.DAla; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hey-NH.sub.2; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; at P.sup.2 with the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain Glu; or Asp; at P.sup.2 with the side chain of Dab; Dap; Dab-NH.sub.2; or Dap-NH.sub.2; at P.sup.11; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; Lys; Dab-NH.sub.2; Dap-NH.sub.2; or Lys-NH.sub.2; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is Ala; Ser; Thr; Dab; Glu; Ser-NH.sub.2; Dab-NH.sub.2; Ala-NH.sub.2; Thr-NH.sub.2; or Glu-NH.sub.2; with the proviso that, if P.sup.3 is Ser; Thr; or Val; then P.sup.1; or P.sup.10; is Tyr; and if P.sup.8 is Val; then P.sup.10 is Trp; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=1, t=0, and u=0; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; Hcy; Ac-Cys; Ac-Pen; or Ac-Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hcy-NH.sub.2; by a disulfide linkage; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; with the side chain of Glu; or Asp; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; P.sup.1 is Val; NMeVal; .sup.DVal; Leu; Ile; Nle; Phe; Tyr; Ser; Leu(3R)OH; Nva; HOVal; Ac-Val; Ac-.sup.DVal; Ac-Leu; Ac-Ile; Ac-Phe; Prop-Val; Ac-Nle; Ac-Tyr; Ac-Ser; Ac-Leu(3R)OH; Ac-Nva; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; X.sup.12 is Val; Ser; Thr; Dab; Tyr; Serol; Throl; .sup.DThrol; Tyrol; Glyol; Val-NH.sub.2; Ser-NH.sub.2; Ser-NHMe; Ser-OiPr; Thr-NH.sub.2; Leu(3R)OH; Asn; Dab-NH.sub.2; or Tyr-NH.sub.2; with the proviso that, if P.sup.1 is Ser; Ac-Ser; Leu(3R)OH; or Ac-Leu(3R)OH; then X.sup.12 is Val; Val-NH.sub.2; Ser-NH.sub.2; Ser-NHMe; Ser-OiPr; Thr-NH.sub.2; or Leu(3R)OH; and if P.sup.3 is Ser; Thr; or Val; then P.sup.1; is Tyr; or Ac-Tyr; or P.sup.10 is Tyr; or X.sup.12 is Tyr; Tyrol; or Tyr-NH.sub.2; and if P.sup.8 is Val; then P.sup.10 is Trp; and if P.sup.10 is Ser; then X.sup.12 is Val; or Val-NH.sub.2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hcy-NH.sub.2; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; at P.sup.2 with the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain Glu; or Asp; at P.sup.2 with the side chain of Dab; Dap; Dab-NH.sub.2; or Dap-NH.sub.2; at P.sup.11; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; Lys; Dab-NH.sub.2; Dap-NH.sub.2; or Lys-NH.sub.2; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; P.sup.1 is Val; NMeVal; .sup.DVal; Leu; Ile; Nle; Phe; Tyr; Ser; Leu(3R)OH; Nva; HOVal; Ac-Val; Ac-.sup.DVal; Ac-Leu; Ac-Ile; Ac-Phe; Prop-Val; Ac-Nle; Ac-Tyr; Ac-Ser; Ac-Leu(3R)OH; Ac-Nva; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is Ala; Ser; Thr; Dab; Glu; Ser-NH.sub.2; Dab-NH.sub.2; Ala-NH.sub.2; Thr-NH.sub.2; or Glu-NH.sub.2; with the proviso that, if P.sup.3 is Ser; Thr; or Val; then P.sup.1; is Tyr; or Ac-Tyr; or P.sup.10 is Tyr; and if P.sup.8 is Val; then P.sup.10 is Trp; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; P.sup.1 is Val; NMeVal; .sup.DVal; Leu; Ile; Nle; Phe; Tyr; Ser; Leu(3R)OH; Nva; HOVal; Ac-Val; Ac-.sup.DVal; Ac-Leu; Ac-Ile; Ac-Phe; Prop-Val; Ac-Nle; Ac-Tyr; Ac-Ser; Ac-Leu(3R)OH; Ac-Nva; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2 is Orn; or Dab; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is .sup.DThr; .sup.DHse; .sup.DAsn; .sup.DGln; .sup.DGlu; .sup.DVal; .sup.DTyr; .sup.DDab; .sup.DOrn; or .sup.DLys; with the proviso that, if P.sup.3 is Ser; Thr; or Val; then P.sup.1; is Tyr; or Ac-Tyr; or P.sup.10 is Tyr; and if P.sup.8 is Val; then P.sup.10 is Trp; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; for module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, Q.sup.1 is Dab; Q.sup.2, Q.sup.5 and Q.sup.6 are Dab; Q.sup.3 is .sup.DLeu; or ° Phe; Q.sup.4 is Leu; Ile; Leu(3R)OH; Abu; Nva; Thr; or alloThr; Q.sup.7 is Thr; or Leu; for a linker L consisting of k=1 or 3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, if k=1, L.sup.1 is .sup.DDab; If k=3, L.sup.1 is Dab; .sup.DDab; .sup.DDap; or NMeDab; L.sup.2 is Thr; Hse; or Ser; L.sup.3 is Dap; Dab; .sup.DDab; or .sup.DDap; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of 0′ and, if k=1 or 3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the nitrogen (N) of L.sup.1; or a pharmaceutically acceptable salt thereof.

    6. Compounds according to any one of claims 1 to 5 wherein specifically for module A, s=0, t=0, and u=0; or s=1, t=0, and u=0; or s=0, t=0, and u=1; if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hey-NH.sub.2; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; at P.sup.2 with the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain Glu; or Asp; at P.sup.2 with the side chain of Dab; Dap; Dab-NH.sub.2; or Dap-NH.sub.2; at P.sup.11; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; Lys; Dab-NH.sub.2; Dap-NH.sub.2; or Lys-NH.sub.2; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; X.sup.14; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined for module A in claim 5, wherein s=1, t=1, and u=1; P.sup.11 is Ala; Ser; Thr; Dab; Glu; Ser-NH.sub.2; Dab-NH.sub.2; Ala-NH.sub.2; Thr-NH.sub.2; or Glu-NH.sub.2; with the proviso that, if P.sup.3 is Ser; Thr; or Val; then P.sup.1; or P.sup.10; is Tyr; and if P.sup.8 is Val; then P.sup.10 is Trp; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=1, t=0, and u=0; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; Hcy; Ac-Cys; Ac-Pen; or Ac-Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hcy-NH.sub.2; by a disulfide linkage; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; with the side chain of Glu; or Asp; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; P.sup.1 is Val; NMeVal; .sup.DVal; Leu; Ile; Nle; Phe; Tyr; Ser; Leu(3R)OH; Nva; HOVal; Ac-Val; Ac-.sup.DVal; Ac-Leu; Ac-Ile; Ac-Phe; Prop-Val; Ac-Nle; Ac-Tyr; Ac-Ser; Ac-Leu(3R)OH; Ac-Nva; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined for module A in claim 5, wherein s=1, t=1, and u=1; X.sup.12 is Val; Ser; Thr; Dab; Tyr; Serol; Throl; .sup.DThrol; Tyrol; Glyol; Val-NH.sub.2; Ser-NH.sub.2; Ser-NHMe; Ser-OiPr; Thr-NH.sub.2; Leu(3R)OH; Asn; Dab-NH.sub.2; or Tyr-NH.sub.2; with the proviso that, if P.sup.1 is Ser; Ac-Ser; Leu(3R)OH; or Ac-Leu(3R)OH; then X.sup.12 is Val; Val-NH.sub.2; Ser-NH.sub.2; Ser-NHMe; Ser-OiPr; Thr-NH.sub.2; or Leu(3R)OH; and if P.sup.3 is Ser; Thr; or Val; then P.sup.1; is Tyr; or Ac-Tyr; or P.sup.10 is Tyr; or X.sup.12 is Tyr; Tyrol; or Tyr-NH.sub.2; and if P.sup.8 is Val; then P.sup.10 is Trp; and if P.sup.10 is Ser; then X.sup.12 is Val; or Val-NH.sub.2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hcy-NH.sub.2; by a disulfide linkage; or connection of the side chain of Dab; Dab(Me); or Dap; at P.sup.2 with the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain Glu; or Asp; at P.sup.2 with the side chain of Dab; Dap; Dab-NH.sub.2; or Dap-NH.sub.2; at P.sup.11; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; Lys; Dab-NH.sub.2; Dap-NH.sub.2; or Lys-NH.sub.2; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; P.sup.1 is Val; NMeVal; .sup.DVal; Leu; Ile; Nle; Phe; Tyr; Ser; Leu(3R)OH; Nva; HOVal; Ac-Val; Ac-.sup.DVal; Ac-Leu; Ac-Ile; Ac-Phe; Prop-Val; Ac-Nle; Ac-Tyr; Ac-Ser; Ac-Leu(3R)OH; Ac-Nva; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined for module A in claim 5, wherein s=1, t=1, and u=1; P.sup.11 is Ala; Ser; Thr; Dab; Glu; Ser-NH.sub.2; Dab-NH.sub.2; Ala-NH.sub.2; Thr-NH.sub.2; or Glu-NH.sub.2; with the proviso that, if P.sup.3 is Ser; Thr; or Val; then P.sup.1; is Tyr; or Ac-Tyr; or P.sup.10 is Tyr; and if P.sup.8 is Val; then P.sup.10 is Trp; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; P.sup.1 is Val; NMeVal; .sup.DVal; Leu; Ile; Nle; Phe; Tyr; Ser; Leu(3R)OH; Nva; HOVal; Ac-Val; Ac-.sup.DVal; Ac-Leu; Ac-Ile; Ac-Phe; Prop-Val; Ac-Nle; Ac-Tyr; Ac-Ser; Ac-Leu(3R)OH; Ac-Nva; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2 is Orn; or Dab; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined for module A in claim 5, wherein s=1, t=1, and u=1; P.sup.11 is .sup.DThr; .sup.DHse; .sup.DAsn; .sup.DGln; .sup.DGlu; .sup.DVal; .sup.DTyr; .sup.DDab; .sup.DOrn; or .sup.DLys; with the proviso that, if P.sup.3 is Ser; Thr; or Val; then P.sup.1; is Tyr; or Ac-Tyr; or P.sup.10 is Tyr; and if P.sup.8 is Val; then P.sup.10 is Trp; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; for module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, Q.sup.1 is Dab; Q.sup.2, Q.sup.5 and Q.sup.6 are Dab; Q.sup.3 is .sup.DLeu; or .sup.DPhe; Q.sup.4 is Leu; Ile; Leu(3R)OH; Abu; Nva; Thr; or alloThr; Q.sup.7 is Thr; or Leu; for a linker L consisting of k=1 or 3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, if k=1, L.sup.1 is .sup.DDab; If k=3, L.sup.1 is Dab; .sup.DDab; .sup.DDap; or NMeDab; L.sup.2 is Thr; Hse; or Ser; L.sup.3 is Dap; Dab; .sup.DDab; or .sup.DDap; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=1 or 3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the nitrogen (N) of L.sup.1; or a pharmaceutically acceptable salt thereof.

    7. Compounds according to any one of claims 1 to 7 wherein specifically for module A, if s=1, t=1, and u=1; and X.sup.14 and X.sup.13 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Ac-Cys; or 3MPA with the side chain of Cys-NH.sub.2 by a disulfide linkage; or connection of the side chain of Ac-Dab; at X.sup.14 with the side chain of Glu-NH.sub.2; at X.sup.13; by a lactam linkage; or X.sup.14 and X.sup.13 taken together form a salt bridge based on the electrostatic interaction between the side chain of Ac-Dab at X.sup.14 and the side chain of Glu-NH.sub.2 at X.sup.13; or the side chain of Ac-Glu at X.sup.14 and the side chain of Dab-NH.sub.2 at X.sup.13; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; at P.sup.2 and the side chain of Glu; at P.sup.11; X.sup.14 is .sup.DSer; pGlu; or .sup.DpGlu; P.sup.1 is Val; Leu; or Leu(3R)OH; P.sup.2 is Thr; P.sup.3 is Tyr; P.sup.4 is Dab; Dap; Ser; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Hse; Thr; Dab; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Glu; Ala; or Gly; P.sup.10 is Val; or tBuGly; Ile; or Nva; P.sup.11 is Ala; or Ser; X.sup.12 is Val; Ser; or Thr; X.sup.13 is .sup.DAla; .sup.DSer; .sup.DAla-N H.sub.2; or .sup.DSer-NH.sub.2; with the proviso that, if P.sup.1 is Leu(3R)OH; then X.sup.12 is Val; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; then P.sup.5 is Glu; if s=1, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; X.sup.14 is pGu; .sup.DpGlu; Ac-Dab; or 6MeHeptA; P.sup.1 is Val; Leu; or Leu(3R)OH; P.sup.2 is Thr; P.sup.3 is Tyr; P.sup.4 is Dap; Dab; Ser; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Thr; Dab; Hse; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Ala; or Gly; P.sup.10 is Val; tBuGly; Ile; or Nva; P.sup.11 is Ala; X.sup.12 is Val-N H.sub.2; Ser-NH.sub.2; Thr-NH.sub.2; Throl; Glyol; Val; Ser; or Thr; with the proviso that, if P.sup.1 is Leu(3R)OH; then X.sup.12 is Val; or Val-NH.sub.2; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; then P.sup.5 is Glu; if s=1, t=1, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; P.sup.1 is Val; HOVal; or Ac-Val; P.sup.2 is Thr; P.sup.3 is Val; Ser; or Thr; P.sup.4 is Dab; Dap; Ser; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Hse; Ser; Thr; Dab; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Ala; or Gly; P.sup.10 is tBuGly; Val; Ile; or Nva; P.sup.11 is Ala; or Ser; X.sup.12 is Tyr; Ala; Gly; or .sup.DAla; X.sup.13 is Glyol; .sup.DAla; .sup.DSer; .sup.DThr; .sup.DAsp; .sup.DAla-NH.sub.2; .sup.DSer-NH.sub.2; Asp; or Asn; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; then P.sup.5 is Glu; if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; X.sup.14 is Ac-Dab; pGlu; or .sup.DpGlu; P.sup.1 is Val; Leu; or Leu(3R)OH; P.sup.2 is Thr; P.sup.3 is Tyr; P.sup.4 is Dap; Dab; Ser; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Hse; Thr; Dab; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Ala; or Gly; P.sup.10 is tBuGly; Val; Ile; or Nva; P.sup.11 is Dab-NH.sub.2; Ala-NH.sub.2; Dab; or Ala; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; then P.sup.5 is Glu; if s=1, t=0, and u=0; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Ac-Pen; with the side chain of Cys-NH.sub.2; by a disulfide linkage; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; hCys; or Pen; with the side chain of Cys; or Pen; by a disulfide linkage; or connection of the side chain of Dab; or Dab(Me); with the side chain of Asp; or Glu; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Asp; or Glu; at P.sup.2 and the side chain of Lys; or Dab; at P.sup.11; or the side chain of Dab at P.sup.2 and the side chain of Asp; or Glu; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; or Pen; with the side chain of Cys; or Pen; by a disulfide linkage; or connection of the side chain of Dab; with the side chain of Asp; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Glu; at P.sup.4 and the side chain of Dap; at P.sup.9; or the side chain of Dab; or Lys; at P.sup.4 and the side chain of Asp; or Glu; at P.sup.9; P.sup.1 is Val; Ac-Val; NMeVal; HOVal; Ac-.sup.DVal; Prop-Val; Leu; Nle; Ac-Nle; Tyr; Ac-Tyr; Ser; Ac-Ser; Ac-Leu(3R)OH; pGlu; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2 is Ala; Val; tBuGly; Dab; Dap; or Thr; P.sup.3 is Val; Ser; Thr; or Tyr; P.sup.4 is Dab; Dap; Ser; Thr; His; or Gly P.sup.5 is Gly; Ala; Val; Abu; His; Thr; or Orn; P.sup.6 is Gly; .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or .sup.DArg; P.sup.7 is Ser; Hse; Thr; Dab; Dap; Ala; or Gly; P.sup.8 is Trp; or Val; P.sup.9 is Ser; Thr; Hse; Glu; Ala; His; Dab; alloThr; or Gly; P.sup.10 is tBuGly; Val; Ile; Nva; Tyr; or Trp; P.sup.11 is Ala; Ser; Thr; Glu; or Dab; X.sup.12 is Glyol; Ser; Serol; Ser-NH.sub.2; Ser-NHMe; Ser-OiPr; Thr-NH.sub.2; Leu(3R)OH; Asn; Throl; .sup.DThrol; Val-NH.sub.2; Tyr-NH.sub.2; Tyrol; or Dab-NH.sub.2; with the proviso that, if P.sup.1 is Ser; Ac-Leu(3R)OH; or Ac-Ser; then X.sup.12 is Val-NH.sub.2; or Leu(3R)OH; and if P.sup.3 is Ser; Thr; or Val; then P.sup.1 is Tyr; or Ac-Tyr; or P.sup.10 is Tyr; or X.sup.12 is Tyr-NH.sub.2; or Tyrol; and if P.sup.8 is Val; then P.sup.10 is Trp; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then; P.sup.5; P.sup.6; or P.sup.7 is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys with the side chain of Cys by a disulfide linkage; P.sup.1 is Ac-Val; NMeVal; HOVal; or Val; P.sup.2 is Thr; P.sup.3 is Tyr; P.sup.4 is Dab; Dap; Ser; Thr; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Hse; Thr; Dab; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Ala; or Gly; P.sup.10 is tBuGly; Val; Ile; or Nva; P.sup.11 is Ser-NH.sub.2; Ser; Ala; or Ala-NH.sub.2; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5 then P.sup.5 is Glu; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; P.sup.1 is Ac-Val; HOVal; Ac-Leu; Ac-Ile; Ac-Nle; or Ac-Phe; Val; Leu; Ile; Nle; or Phe; P.sup.2 is Orn; or Dab; P.sup.3 is Tyr; P.sup.4 is Dab; Dap; Ser; Thr; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Hse; Thr; Dab; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Ala; or Gly; P.sup.10 is tBuGly; Val; Ile; or Nva; P.sup.11 is .sup.DThr; .sup.DHse; .sup.DAsn; .sup.DGln; .sup.DGlu; .sup.DVal; .sup.DTyr; .sup.DDab; ° Orn; or .sup.DLys; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5 then P.sup.5 is Glu; or a pharmaceutically acceptable salt thereof.

    8. Compounds according to any one of claims 1 to 7 wherein specifically for module A, s=0, t=0, and u=0; or s=1, t=0, and u=0; or s=0, t=0, and u=1 if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; X.sup.14 is Ac-Dab; pGlu; or .sup.DpGlu; P.sup.1 is Val; Leu; or Leu(3R)OH; P.sup.2 is Thr; P.sup.3 is Tyr; P.sup.4 is Dap; Dab; Ser; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Hse; Thr; Dab; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Ala; or Gly; P.sup.10 is tBuGly; Val; Ile; or Nva; P.sup.11 is Dab-NH.sub.2; Ala-NH.sub.2; Dab; or Ala; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; then P.sup.5 is Glu; if s=1, t=0, and u=0; and P.sup.1 and X.sup.12 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Ac-Pen; with the side chain of Cys-NH.sub.2; by a disulfide linkage; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; hCys; or Pen; with the side chain of Cys; or Pen; by a disulfide linkage; or connection of the side chain of Dab; or Dab(Me); with the side chain of Asp; or Glu; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Asp; or Glu; at P.sup.2 and the side chain of Lys; or Dab; at P.sup.11; or the side chain of Dab at P.sup.2 and the side chain of Asp; or Glu; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; or Pen; with the side chain of Cys; or Pen; by a disulfide linkage; or connection of the side chain of Dab; with the side chain of Asp; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Glu; at P.sup.4 and the side chain of Dap; at P.sup.9; or the side chain of Dab; or Lys; at P.sup.4 and the side chain of Asp; or Glu; at P.sup.9; P.sup.1 is Val; Ac-Val; NMeVal; HOVal; Ac-.sup.DVal; Prop-Val; Leu; Nle; Ac-Nle; Tyr; Ac-Tyr; Ser; Ac-Ser; Ac-Leu(3R)OH; pGlu; 3MeButA; 2MePropA; or 6MeHeptA; P.sup.2 is Ala; Val; tBuGly; Dab; Dap; or Thr; P.sup.3 is Val; Ser; Thr; or Tyr; P.sup.4 is Dab; Dap; Ser; Thr; His; or Gly P.sup.5 is Gly; Ala; Val; Abu; His; Thr; or Orn; P.sup.6 is Gly; .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or .sup.DArg; P.sup.7 is Ser; Hse; Thr; Dab; Dap; Ala; or Gly; P.sup.8 is Trp; or Val; P.sup.9 is Ser; Thr; Hse; Glu; Ala; His; Dab; alloThr; or Gly; P.sup.10 is tBuGly; Val; Ile; Nva; Tyr; or Trp; P.sup.11 is Ala; Ser; Thr; Glu; or Dab; X.sup.12 is Glyol; Ser; Serol; Ser-NH.sub.2; Ser-NHMe; Ser-OiPr; Thr-NH.sub.2; Leu(3R)OH; Asn; Throl; .sup.DThrol; Val-NH.sub.2; Tyr-NH.sub.2; Tyrol; or Dab-NH.sub.2; with the proviso that, if P.sup.1 is Ser; Ac-Leu(3R)OH; or Ac-Ser; then X.sup.12 is Val-NH.sub.2; or Leu(3R)OH; and if P.sup.3 is Ser; Thr; or Val; then P.sup.1 is Tyr; or Ac-Tyr; or P.sup.10 is Tyr; or X.sup.12 is Tyr-NH.sub.2; or Tyrol; and if P.sup.8 is Val; then P.sup.10 is Trp; and the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if P.sup.1 and X.sup.12 taken together form an interstrand linkage or salt bridge, as defined above; then P.sup.2 and P.sup.11 taken together are not forming an interstrand linkage or salt bridge, as defined above; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then; P.sup.5; P.sup.6; or P.sup.7 is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys with the side chain of Cys by a disulfide linkage; P.sup.1 is Ac-Val; NMeVal; HOVal; or Val; P.sup.2 is Thr; P.sup.3 is Tyr; P.sup.4 is Dab; Dap; Ser; Thr; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Hse; Thr; Dab; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Ala; or Gly; P.sup.10 is tBuGly; Val; Ile; or Nva; P.sup.11 is Ser-NH.sub.2; Ser; Ala; or Ala-NH.sub.2; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5 then P.sup.5 is Glu; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; P.sup.1 is Ac-Val; HOVal; Ac-Leu; Ac-Ile; Ac-Nle; or Ac-Phe; Val; Leu; Ile; Nle; or Phe; P.sup.2 is Orn; or Dab; P.sup.a is Tyr; P.sup.4 is Dab; Dap; Ser; Thr; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Ser; Hse; Thr; Dab; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Ser; Hse; Ala; or Gly; P.sup.10 is tBuGly; Val; Ile; or Nva; P.sup.11 is .sup.DThr; .sup.DHse; .sup.DAsn; .sup.DGln; .sup.DGlu; .sup.DVal; .sup.DTyr; .sup.DDab; ° Orn; or .sup.DLys; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5 then P.sup.5 is Glu; or a pharmaceutically acceptable salt thereof.

    9. Compounds according to any one of claims 1 to 6 wherein specifically for module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, Q.sup.1 is Dab; Q.sup.2, Q.sup.5 and Q.sup.6 are Dab; Q.sup.3 is .sup.DLeu; or .sup.DPhe; Q.sup.4 is Leu; Ile; Leu(3R)OH; Abu; Nva; Thr; or alloThr; Q.sup.7 is Thr; or Leu; or a pharmaceutically acceptable salt thereof.

    10. Compounds according to any one of claims 1 to 6 wherein specifically for a linker L consisting of k=1 or 3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, if k=1, L.sup.1 is .sup.DDab; If k=3, L.sup.1 is Dab; .sup.DDab; .sup.DDap; or NMeDab; L.sup.2 is Thr; Hse; or Ser; L.sup.3 is Dap; Dab; .sup.DDab; or .sup.DDap; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=1 or 3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; to the nitrogen (N) of L.sup.1; or a pharmaceutically acceptable salt thereof.

    11. Compounds according to any one of claims 1 to 10 wherein specifically for module A, if s=1, t=1, and u=1; and X.sup.14 and X.sup.13 taken together form an interstrand linking bis(amino acid)-structure or (amino acid)-(acid) structure based on the linkage of two L amino acid residues; or an amino acid residue and an acid residue; following connection of the side chain of Cys; Pen; Hcy; Ac-Cys; Ac-Pen; Ac-Hcy; or 3MPA with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2 Pen-NH.sub.2; or Hey-NH.sub.2; by a disulfide linkage; or connection of the side chain of Ac-Dab; Ac-Dap; Dab; or Dap; at X.sup.14 with the side chain of Glu-NH.sub.2; Asp-NH.sub.2; Glu; or Asp; at X.sup.13; or the side chain of Ac-Glu; Ac-Asp; Glu; or Asp; at X.sup.14 with the side chain of Dab-NH.sub.2; Dap-NH.sub.2; Dab; or Dap; at X.sup.13; by a lactam linkage; or X.sup.14 and X.sup.13 taken together form a salt bridge based on the electrostatic interaction between the side chain of Ac-Dab; Ac-Dap; Ac-Lys; Dab; Dap; or Lys; at X.sup.14 and the side chain of Glu-NH.sub.2; Asp-NH.sub.2; Glu; or Asp; at X.sup.13; or the side chain of Ac-Glu; Ac-Asp; Glu; or Asp; at X.sup.14 and the side chain of Dab-NH.sub.2; Dap-NH.sub.2; Lys-NH.sub.2; Dab; Dap; or Lys; at X.sup.13; and/or P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; or Dap; at P.sup.2 with the side chain of Glu; or Asp; at P.sup.11; or the side chain Glu; or Asp; at P.sup.2 with the side chain of Dab; or Dap; at P.sup.11; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; X.sup.14 is .sup.DSer; P.sup.1 is Val; P.sup.2 is Thr; P.sup.3 is Tyr; P.sup.4 is Ser; Dap; Dap; or Gly; P.sup.5 is Orn; His; or Gly; P.sup.6 is .sup.DDab; .sup.DSer; .sup.DHse; .sup.DAla; or Gly; P.sup.7 is Dab; Thr; Ser; Hse; Ala; or Gly; P.sup.8 is Trp; P.sup.9 is Glu; Ala; Dab; Ser; or Hse; P.sup.10 is tBuGly; Val; or Ile P.sup.11 is Ala; or Ser; X.sup.12 is Thr; X.sup.13 is .sup.DAla; or .sup.DSer; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=1, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; or Dap; with the side chain of Glu; or Asp; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P9; X.sup.14 is pGu; or .sup.DpGlu; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; X.sup.12 is Throl; Thr-NH.sub.2; or Thr; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=1, t=1, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys by a disulfide linkage; P.sup.1 is Val; HOVal; or Ac-Val; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 and X.sup.12 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; X.sup.13 is Glyol; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hey-NH.sub.2; by a disulfide linkage; or connection of the side chain of Dab; or Dap; at P.sup.2 with the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain Glu; or Asp; at P.sup.2 with the side chain of Dab; Dap; Dab-NH.sub.2; or Dap-NH.sub.2; at P.sup.11; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; Lys; Dab-NH.sub.2; Dap-NH.sub.2; or Lys-NH.sub.2; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; X.sup.14 is Ac-Dab; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is Dab-NH.sub.2; or Dab; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=1, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; or Dap; with the side chain of Glu; or Asp; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; P.sup.1 is Val; Ac-Val; NMeVal; HOVal; Prop-Val; Ac-Nle; Ac-Tyr; Nle; or Tyr; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10; are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is Ala; Ser; Thr; Glu; or Dab; X.sup.12 is Glyol; Ser; Serol; Ser-NH.sub.2; Ser-NHMe; Thr; Thr-NH.sub.2; Throl; Val-NH.sub.2; or Tyrol; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys with the side chain of Cys by a disulfide linkage; P.sup.1 is Ac-Val; NMeVal; HOVal; or Val; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is Ser-NH.sub.2; or Ser; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; P.sup.1 is Ac-Val; HOVal; Ac-Leu; Ac-Ile; Ac-Nle; Ac-Phe; Val; Leu; Nle; Ile; or Phe; P.sup.2 is Orn; or Dab; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined above for module A in this claim, wherein s=1, t=1, and u=1; P.sup.11 is .sup.DThr; .sup.DHse; .sup.DAsn; .sup.DGln; .sup.DGlu; .sup.DVal; .sup.DTyr; .sup.DDab; .sup.DOrn; or .sup.DLys; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; for module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, Q.sup.1 is Dab; Q.sup.2, Q.sup.5 and Q.sup.6 are Dab; Q.sup.3 is .sup.DLeu; Q.sup.4 is Leu; Q.sup.7 is Thr; for a linker L consisting of k=3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, L.sup.1 is Dab; or .sup.DDab; L.sup.2 is Thr; L.sup.3 is Dap; or Dab; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5 to the nitrogen (N) of L.sup.1; or a pharmaceutically acceptable salt thereof.

    12. Compounds according to any one of claims 1 to 11 wherein specifically for module A, s=0, t=0, and u=0; or s=1, t=0, and u=0; or s=0, t=0, and u=1 if s=0, t=0, and u=1; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; Hcy; Cys-NH.sub.2; Pen-NH.sub.2; or Hey-NH.sub.2; by a disulfide linkage; or connection of the side chain of Dab; or Dap; at P.sup.2 with the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain Glu; or Asp; at P.sup.2 with the side chain of Dab; Dap; Dab-NH.sub.2; or Dap-NH.sub.2; at P.sup.11; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; Asp; Glu-NH.sub.2; or Asp-NH.sub.2; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; Lys; Dab-NH.sub.2; Dap-NH.sub.2; or Lys-NH.sub.2; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; X.sup.14 is Ac-Dab; P.sup.1; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined for module A in claim 11, wherein s=1, t=1, and u=1; P.sup.11 is Dab-NH.sub.2; or Dab; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=1, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Dab; or Dap; with the side chain of Glu; or Asp; by a lactam linkage; or P.sup.2 and P.sup.11 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.2 and the side chain of Glu; or Asp; at P.sup.11; or the side chain of Glu; or Asp; at P.sup.2 and the side chain of Dab; Dap; or Lys; at P.sup.11; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; Pen; or Hcy; with the side chain of Cys; Pen; or Hcy; by a disulfide linkage; or connection of the side chain of Asp; or Glu; with the side chain of Dab; or Dap; by a lactam linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab; Dap; or Lys; at P.sup.4 and the side chain of Glu; or Asp; at P.sup.9; or the side chain of Glu; or Asp; at P.sup.4 and the side chain of Dab; Dap; or Lys; at P.sup.9; P.sup.1 is Val; Ac-Val; NMeVal; HOVal; Prop-Val; Ac-Nle; Ac-Tyr; Nle; or Tyr; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10; are as defined for module A in claim 11, wherein s=1, t=1, and u=1; P.sup.11 is Ala; Ser; Thr; Glu; or Dab; X.sup.12 is Glyol; Ser; Serol; Ser-NH.sub.2; Ser-NHMe; Thr; Thr-NH.sub.2; Throl; Val-NH.sub.2; or Tyrol; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys with the side chain of Cys by a disulfide linkage; and/or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys with the side chain of Cys by a disulfide linkage; P.sup.1 is Ac-Val; NMeVal; HOVal; or Val; P.sup.2; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; P.sup.10; and P.sup.11 are as defined for module A in claim 11, wherein s=1, t=1, and u=1; P.sup.11 is Ser-NH.sub.2; or Ser; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu; if s=0, t=0, and u=0; and alternatively P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; P.sup.1 is Ac-Val; HOVal; Ac-Leu; Ac-Ile; Ac-Nle; Ac-Phe; Val; Leu; Nle; Ile; or Phe; P.sup.2 is Orn; or Dab; P.sup.3; P.sup.4; P.sup.5; P.sup.6; P.sup.7; P.sup.8; P.sup.9; and P.sup.10 are as defined for module A in claim 11, wherein s=1, t=1, and u=1; P.sup.11 is .sup.DThr; .sup.DHse; .sup.DAsn; .sup.DGln; .sup.DGlu; .sup.DVal; .sup.DTyr; .sup.DDab; .sup.DOrn; or .sup.DLys; with the proviso that, the combined number of the amino acid residue Gly in above module A must not exceed two; and the positions P of the amino acid residues Gly must not be in direct vicinity; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; P.sup.6; or P.sup.7; then P.sup.5; P.sup.6; or P.sup.7; is Glu; or .sup.DGlu for module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, Q.sup.1 is Dab; Q.sup.2, Q.sup.5 and Q.sup.6 are Dab; Q.sup.3 is .sup.DLeu; Q.sup.4 is Leu; Q.sup.7 is Thr; for a linker L consisting of k=3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, L.sup.1 is Dab; or .sup.DDab; L.sup.2 is Thr; L.sup.3 is Dap; or Dab; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5 to the nitrogen (N) of L.sup.1; or a pharmaceutically acceptable salt thereof.

    13. Compounds according to any one of claims 1 to 10 wherein specifically for module A, s=1, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys; by a disulfide linkage; or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys; or Pen; by a disulfide linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab at P.sup.4 and the side chain of Glu; at P.sup.9; P.sup.1 is Val; Ac-Val; NMeVal; HOVal; Ac-Nle; or Ac-Tyr; P.sup.2 is Thr; P.sup.3 is Val; Ser; or Tyr; P.sup.4 is Dab; Dap; Thr; or Ser; P.sup.5 is Orn; Ala; Val; Abu; His; or Thr; P.sup.6 is .sup.DDab; .sup.DSer; or .sup.DHse; P.sup.7 is Ser; Hse; Thr; or Dab; P.sup.8 is Trp; P.sup.9 is Ser; Hse; alloThr; Dab; or Glu; P.sup.10 is tBuGly; Val; or Ile; P.sup.11 is Ala; X.sup.12 is Ser; Serol; Ser-NH.sub.2; Thr-NH.sub.2; Throl; Tyr-NH.sub.2; Asn; or Tyrol; with the proviso that, if P.sup.3 is Ser; or Val; then P.sup.1 is Ac-Tyr; or X.sup.12 is Tyr-NH.sub.2; or Tyrol; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; or P.sup.6; then; P.sup.5; is Glu; or P.sup.6 is .sup.DGlu; for module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, Q.sup.1 is Dab; Q.sup.2, Q.sup.5 and Q.sup.6 are Dab; Q.sup.3 is .sup.DLeu; Q.sup.4 is Leu; Ile; Abu; or Thr; Q.sup.7 is Thr; for a linker L consisting of k=3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, L.sup.1 is Dab; or .sup.DDab; L.sup.2 is Thr; or Ser; L.sup.3 is Dap; Dab; or .sup.DDab; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; or P.sup.6; to the nitrogen (N) of L.sup.1; or a pharmaceutically acceptable salt thereof.

    14. Compounds according to any one of claims 1 to 10, or claim 13, wherein specifically for module A, s=1, t=0, and u=0; and P.sup.2 and P.sup.11 taken together form an interstrand linking bis(amino acid)-structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys; by a disulfide linkage; or P.sup.4 and P.sup.9 taken together form an interstrand linking bis(amino acid) structure based on the linkage of two L amino acid residues; following connection of the side chain of Cys; with the side chain of Cys; or Pen; by a disulfide linkage; or P.sup.4 and P.sup.9 taken together form a salt bridge based on the electrostatic interaction between the side chain of Dab at P.sup.4 and the side chain of Glu; at P.sup.9; P.sup.1 is Val; Ac-Val; NMeVal; HOVal; Ac-Nle; or Ac-Tyr; P.sup.2 is Thr; P.sup.3 is Val; Ser; or Tyr; P.sup.4 is Dab; or Ser; P.sup.5 is Orn; P.sup.6 is .sup.DDab; or .sup.DSer; P.sup.7 is Ser; Hse; Thr; or Dab; P.sup.8 is Trp; P.sup.9 is Ser; Hse; alloThr; Dab; or Glu; P.sup.10 is Val; or Ile; P.sup.11 is Ala; X.sup.12 is Ser; Ser-NH.sub.2; Thr-NH.sub.2; Tyrol; or Tyr-NH.sub.2; with the proviso that, if P.sup.3 is Ser; or Val; then P.sup.1 is Ac-Tyr; or X.sup.12 is Tyrol; or Tyr-NH.sub.2; with the further proviso that, if P.sup.7 is Dab; then P.sup.4 is Ser and Q.sup.4 of module B is Abu; or Thr; with the further proviso that, if linker L, as defined below, is connected with module A by a carbonyl (C═O) point of attachment of P.sup.5; or P.sup.6; then; P.sup.5; is Glu; or P.sup.6 is .sup.DGlu; for module B consisting of single elements Q being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element with the proviso that Q.sup.7 is connected from the α-carbonyl (C═O) point of attachment to the ω-nitrogen (N) of Q.sup.1, Q.sup.1 is Dab; Q.sup.2, Q.sup.5 and Q.sup.6 are Dab; Q.sup.3 is .sup.DLeu; Q.sup.4 is Leu; Ile; Abu; or Thr; Q.sup.7 is Thr; for a linker L consisting of k=3 single elements L being connected in either direction from the carbonyl (C═O) point of attachment to the nitrogen (N) of the next element, L.sup.1 is Dab; or .sup.DDab; L.sup.2 is Thr; or Ser; L.sup.3 is Dap; Dab; or .sup.DDab; said linker L being connected with module B from the carbonyl (C═O) point of attachment of L.sup.k to the α-nitrogen (N) of Q.sup.1 and, if k=3, being connected with module A from the carbonyl (C═O) point of attachment of P.sup.5; or P.sup.6; to the nitrogen (N) of L.sup.1; or a pharmaceutically acceptable salt thereof.

    15. Compounds according to any one of claims 1 to 14 which are selected from the group consisting of Ex. 1 to 385, the sequences of which are shown in the following Table below: TABLE-US-00009 Ex. No. Sequence Ex 1 .sup.a) b) c) embedded image Ex 2 .sup.a) b) c) embedded image Ex 3 .sup.a) b) c) embedded image Ex 4 .sup.a) b) c) embedded image Ex 5 .sup.a) b) c) embedded image Ex 6 .sup.a) embedded image Ex 7 .sup.a) e) embedded image Ex 8 .sup.a) embedded image Ex 9 .sup.a) embedded image Ex 10 .sup.a) embedded image Ex 11 .sup.a) embedded image Ex 12 .sup.a) embedded image Ex 13 .sup.a) embedded image Ex 14 .sup.a) embedded image Ex 15 .sup.f`) embedded image Ex 16 .sup.f) embedded image Ex 17 .sup.f) embedded image Ex 18 .sup.f) embedded image Ex 19 .sup.f) embedded image Ex 20 .sup.f) embedded image Ex 21 .sup.f) embedded image Ex 22 .sup.f) embedded image Ex 23 .sup.f) embedded image Ex 24 .sup.e) f) embedded image Ex 25 .sup.f) embedded image Ex 26 .sup.f) embedded image Ex 27 .sup.f) embedded image Ex 28 .sup.f) embedded image Ex 29 .sup.f) embedded image Ex 30 .sup.f) embedded image Ex 31 .sup.f) embedded image Ex 32 .sup.f) embedded image Ex 33 .sup.f) embedded image Ex 34 .sup.f) embedded image Ex 35 .sup.f) embedded image Ex 36 .sup.f) embedded image Ex 37 .sup.f) embedded image Ex 38 .sup.f) embedded image Ex 39 .sup.a) embedded image Ex 40 .sup.a) embedded image Ex 41 .sup.a) embedded image Ex 42 .sup.a) embedded image Ex 43 .sup.a) embedded image Ex 44 .sup.a) embedded image Ex 45 .sup.a) embedded image Ex 46 .sup.a) embedded image Ex 47 .sup.a) embedded image Ex 48 .sup.a) embedded image Ex 49 .sup.a) embedded image Ex 50 .sup.a) embedded image Ex 51 .sup.a) embedded image Ex 52 .sup.a) embedded image Ex 53 .sup.a) embedded image Ex 54 .sup.a) embedded image Ex 55 .sup.g) embedded image Ex 56 .sup.g) embedded image Ex 57 .sup.a) embedded image Ex 58 .sup.a) h) embedded image Ex 59 .sup.a) h) embedded image Ex 60 .sup.a) h) embedded image Ex 61 .sup.a) h) embedded image Ex 62 .sup.a) embedded image Ex 63 .sup.a) embedded image Ex 64 .sup.a) embedded image Ex 65 .sup.a) embedded image Ex 66 .sup.a) embedded image Ex 67 .sup.a) embedded image Ex 68 .sup.a) embedded image Ex 69 .sup.a) h) embedded image Ex 70 .sup.a) h) embedded image Ex 71 .sup.a) b) embedded image Ex 72 .sup.a) h) embedded image Ex 73 .sup.a) h) embedded image Ex 74 .sup.a) h) embedded image Ex 75 .sup.a) h) embedded image Ex 76 .sup.a) h) embedded image Ex 77 .sup.a) b) embedded image Ex 78 .sup.a) h) embedded image Ex 79 .sup.a) h) embedded image Ex 80 .sup.a) h) embedded image Ex 81 .sup.a) h) embedded image Ex 82 .sup.a) h) embedded image Ex 83 .sup.a) h) embedded image Ex 84 .sup.a) h) embedded image Ex 85 .sup.a) h) embedded image Ex 86 .sup.a) b) embedded image Ex 87 .sup.a) h) embedded image Ex 88 .sup.a) h) embedded image Ex 89 .sup.a) h) embedded image Ex 90 .sup.a) h) embedded image Ex 91 .sup.a) h) embedded image Ex 92 .sup.a) h) embedded image Ex 93 .sup.a) h) embedded image Ex 94 .sup.a) b) embedded image Ex 95 .sup.a) b) embedded image Ex 96 .sup.a) b) embedded image Ex 97 .sup.a) h) embedded image Ex 98 .sup.a) b) embedded image Ex 99 .sup.a) e) embedded image Ex 100 .sup.a) embedded image Ex 101 .sup.a) h) embedded image Ex 102 .sup.a) h) embedded image Ex 103 .sup.a) h) embedded image Ex 104 .sup.a) h) embedded image Ex 105 .sup.a) h) embedded image Ex 106 .sup.a) h) embedded image Ex 107 .sup.a) h) embedded image Ex 108 .sup.a) h) embedded image Ex 109 .sup.a) h) embedded image Ex 110 .sup.a) h) embedded image Ex 111 .sup.a) h) embedded image Ex 112 .sup.a) h) embedded image Ex 113 .sup.a) embedded image Ex 114 .sup.a) embedded image Ex 115 .sup.a) e) embedded image Ex 116 .sup.a) b) embedded image Ex 117 .sup.a) embedded image Ex 119 .sup.a) embedded image Ex 120 .sup.a) embedded image Ex 121 .sup.a) embedded image Ex 122 .sup.a) embedded image Ex 123 .sup.a) b) embedded image Ex 124 .sup.a) b) embedded image Ex 125 .sup.a) embedded image Ex 126 .sup.a) embedded image Ex 127 .sup.a) h) embedded image Ex 128 .sup.a) embedded image Ex 129 .sup.a) b) embedded image Ex 130 .sup.a) embedded image Ex 131 .sup.a) embedded image Ex 132 .sup.a) embedded image Ex 133 .sup.a) embedded image Ex 134 .sup.a) embedded image Ex 135 .sup.a) embedded image Ex 136 .sup.a) embedded image Ex 137 .sup.a) embedded image Ex 138 .sup.a) embedded image Ex 139 .sup.a) embedded image Ex 140 .sup.a) embedded image Ex 141 .sup.a) embedded image Ex 142 .sup.a) embedded image Ex 143 .sup.a) embedded image Ex 144 .sup.a) embedded image Ex 145 .sup.a) embedded image Ex 146 .sup.g) embedded image Ex 147 .sup.g) embedded image Ex 148 .sup.g) embedded image Ex 149 .sup.g) embedded image Ex 150 .sup.a) embedded image Ex 151 .sup.a) embedded image Ex 152 .sup.a) embedded image Ex 153 .sup.a) embedded image Ex 154 .sup.a) embedded image Ex 155 .sup.a) embedded image Ex 156 .sup.a) embedded image Ex 157 .sup.a) e) embedded image Ex 158 .sup.a) embedded image Ex 159 .sup.a) embedded image Ex 160 .sup.a) e) embedded image Ex 161 .sup.a) e) embedded image Ex 162 .sup.a) h) embedded image Ex 163 .sup.a) h) embedded image Ex 164 .sup.a) e) embedded image Ex 165 .sup.a) e) embedded image Ex 166 .sup.a) e) embedded image Ex 167 .sup.a) e) embedded image Ex 168 .sup.a) e) embedded image Ex 169 .sup.a) e) embedded image Ex 170 .sup.a) embedded image Ex 171 .sup.a) e) embedded image Ex 172 .sup.a) h) embedded image Ex 173 .sup.a) h) embedded image Ex 174 .sup.a) h) embedded image Ex 175 .sup.a) embedded image Ex 176 .sup.a) embedded image Ex 177 .sup.a) embedded image Ex 178 .sup.a) embedded image Ex 179 .sup.a) embedded image Ex 180 .sup.a) embedded image Ex 181 .sup.a) embedded image Ex 182 .sup.a) embedded image Ex 183 .sup.a) embedded image Ex 184 .sup.a) embedded image Ex 185 .sup.a) embedded image Ex 186 .sup.a) embedded image Ex 187 .sup.g) embedded image Ex 188 .sup.a) h) embedded image Ex 189 .sup.a) h) embedded image Ex 190 .sup.a) h) embedded image Ex 191 .sup.a) h) embedded image Ex 192 .sup.a) h) embedded image Ex 193 .sup.a) h) embedded image Ex 194 .sup.a) h) embedded image Ex 195 .sup.a) h) embedded image Ex 196 .sup.a) b) embedded image Ex 197 .sup.a) h) embedded image Ex 198 .sup.a) h) embedded image Ex 199 .sup.a) h) embedded image Ex 200 .sup.a) h) embedded image Ex 201 .sup.a) h) embedded image Ex 202 .sup.a) h) embedded image Ex 203 .sup.a) h) embedded image Ex 204 .sup.a) h) embedded image Ex 205 .sup.a) embedded image Ex 206 .sup.a) embedded image Ex 207 .sup.a) embedded image Ex 208 .sup.a) embedded image Ex 209 .sup.a) h) embedded image Ex 210 .sup.a) h) embedded image Ex 211 .sup.a) h) embedded image Ex 212 .sup.a) h) embedded image Ex 213 .sup.a) h) embedded image Ex 214 .sup.a) h) embedded image Ex 215 .sup.a) embedded image Ex 216 .sup.a) h) embedded image Ex 217 .sup.a) h) embedded image Ex 218 .sup.a) embedded image Ex 219 .sup.a) embedded image Ex 220 .sup.a) embedded image Ex 221 .sup.a) embedded image Ex 222 .sup.a) embedded image Ex 223 .sup.a) embedded image Ex 224 .sup.a) embedded image Ex 225 .sup.a) embedded image Ex 226 .sup.a) embedded image Ex 227 .sup.a) embedded image Ex 228 .sup.a) embedded image Ex 229 embedded image Ex 230 embedded image Ex 232 .sup.a) b) embedded image Ex 233 .sup.a) b) embedded image Ex 234 .sup.a) embedded image Ex 235 .sup.a) embedded image Ex 236 .sup.a) h) embedded image Ex 237 .sup.a) embedded image Ex 238 .sup.a) embedded image Ex 239 .sup.a) embedded image Ex 240 .sup.a) embedded image Ex 241 .sup.a) embedded image Ex 242 .sup.a) embedded image Ex 243 .sup.a) embedded image Ex 244 .sup.a) embedded image Ex 245 .sup.a) c) i) embedded image Ex 246 .sup.a) embedded image Ex 247 embedded image Ex 248 embedded image Ex 249 embedded image Ex 250 .sup.a) c) i) embedded image Ex 251 .sup.a) embedded image Ex 252 .sup.a) embedded image Ex 253 .sup.a) embedded image Ex 254 .sup.a) embedded image Ex 255 .sup.a) embedded image Ex 256 .sup.a) embedded image Ex 257 .sup.a) embedded image Ex 258 .sup.a) embedded image Ex 259 .sup.a) embedded image Ex 260 .sup.a) embedded image Ex 261 .sup.a) embedded image Ex 262 .sup.a) embedded image Ex 263 .sup.a) embedded image Ex 264 .sup.a) embedded image Ex 265 .sup.g) embedded image Ex 266 .sup.a) embedded image Ex 267 .sup.a) embedded image Ex 268 .sup.a) embedded image Ex 269 .sup.a) embedded image Ex 270 .sup.a) e) embedded image Ex 271 .sup.a) e) embedded image Ex 272 .sup.a) embedded image Ex 273 .sup.g) embedded image Ex 274 .sup.a) e) embedded image Ex 275 .sup.a) embedded image Ex 276 .sup.a) embedded image Ex 277 .sup.a) e) embedded image Ex 278 .sup.a) embedded image Ex 279 .sup.g) embedded image Ex 280 .sup.a) embedded image Ex 281 .sup.a) embedded image Ex 282 .sup.a) embedded image Ex 283 .sup.a) embedded image Ex 284 .sup.a) embedded image Ex 285 .sup.g) embedded image Ex 286 .sup.g) embedded image Ex 287 .sup.g) embedded image Ex 288 .sup.g) embedded image Ex 289 .sup.a) embedded image Ex 290 .sup.a) embedded image Ex 291 .sup.g) embedded image Ex 292 .sup.g) embedded image Ex 293 .sup.g) embedded image Ex 294 .sup.a) embedded image Ex 295 .sup.a) embedded image Ex 296 .sup.a) embedded image Ex 297 .sup.a) embedded image Ex 298 .sup.a) embedded image Ex 299 .sup.a) embedded image Ex 300 .sup.a) embedded image Ex 301 .sup.a) e) embedded image Ex 302 .sup.g) embedded image Ex 303 .sup.g) embedded image Ex 304 .sup.g) e) embedded image Ex 305 .sup.a) embedded image Ex 306 .sup.a) embedded image Ex 307 .sup.a) embedded image Ex 308 .sup.a) embedded image Ex 309 .sup.a) embedded image Ex 310 .sup.a) embedded image Ex 311 .sup.a) embedded image Ex 312 .sup.a) embedded image Ex 313 .sup.a) embedded image Ex 314 .sup.a) embedded image Ex 315 .sup.a) embedded image Ex 316 .sup.a) embedded image Ex 317 .sup.a) embedded image Ex 318 .sup.a) embedded image Ex 319 .sup.g) embedded image Ex 320 .sup.g) embedded image Ex 321 .sup.g) embedded image Ex 322 .sup.g) embedded image Ex 323 .sup.g) embedded image Ex 324 .sup.g) embedded image Ex 325 .sup.g) embedded image Ex 326 .sup.g) embedded image Ex 327 .sup.g) embedded image Ex 328 .sup.a) embedded image Ex 329 .sup.a) embedded image Ex 330 .sup.a) embedded image Ex 331 .sup.a) embedded image Ex 332 .sup.a) embedded image Ex 333 .sup.a) embedded image Ex 334 .sup.a) embedded image Ex 335 .sup.a) embedded image Ex 336 .sup.a) embedded image Ex 337 .sup.a) embedded image Ex 338 .sup.a) embedded image Ex 339 .sup.a) embedded image Ex 340 .sup.a) e) embedded image Ex 341 .sup.a) embedded image Ex 342 .sup.a) embedded image Ex 343 .sup.a) embedded image Ex 344 .sup.a) e) embedded image Ex 345 .sup.a) embedded image Ex 346 .sup.g) embedded image Ex 347 .sup.g) e) embedded image Ex 348 .sup.g) embedded image Ex 349 .sup.g) embedded image Ex 350 .sup.a) embedded image Ex 351 .sup.g) embedded image Ex 352 .sup.a) embedded image Ex 353 .sup.a) embedded image Ex 354 .sup.a) embedded image Ex 355 .sup.a) embedded image Ex 356 .sup.a) embedded image Ex 357 .sup.a) embedded image Ex 358 .sup.a) embedded image Ex 359 .sup.a) embedded image Ex 360 .sup.a) embedded image Ex 361 .sup.a) embedded image Ex 362 .sup.a) embedded image Ex 363 .sup.a) embedded image Ex 364 .sup.a) embedded image Ex 365 .sup.a) embedded image Ex 366 .sup.a) embedded image Ex 367 .sup.a) embedded image Ex 368 .sup.a) embedded image Ex 369 .sup.a) embedded image Ex 370 .sup.a) embedded image Ex 371 .sup.a) embedded image Ex 372 .sup.a) e) embedded image Ex 373 .sup.a) embedded image Ex 374 .sup.a) embedded image Ex 375 .sup.a) embedded image Ex 376 .sup.a) e) embedded image Ex 377 .sup.a) embedded image Ex 378 .sup.a) embedded image Ex 379 .sup.a) e) embedded image Ex 380 .sup.a) embedded image Ex 381 .sup.a) e) embedded image Ex 382 .sup.a) e) embedded image Ex 383 .sup.a) embedded image Ex 384 .sup.a) embedded image Ex 385 .sup.a) embedded image .sup.a) Disulfide interstrand linkage(s) between indicated amino acid residues in module A, involving disulfide bond(s) between a pair(s) of side-chain thiol groups as specified. .sup.b) 1,2-amino alcohol residue attached to the C-terminal amino acid residue of module A, involving an amide bond between the α-carboxyl group of the C-terminal amino acid residue and the amino group of the amino alcohol residue. .sup.c) Acid residue attached to the N-terminal amino acid residue of module A, involving an amide bond between the carboxyl group of the acid residue and the α-amino group of the N-terminal amino acid residue. .sup.e) α-hydroxy acid residue attached to the N-terminal amino acid residue of module A, involving an amide bond between the carboxyl group of the hydroxy acid residue and the α-amino group of the N-terminal amino acid residue. .sup.f) Lactam linkage between the two indicated amino acid residues in module A, involving an amide bond between the side-chain amino group of the residue at P.sup.2 and the α-carboxyl group of the residue at P.sup.11. .sup.g) Lactam interstrand linkage between the two indicated amino acid residues in module A, involving an amide bond between a side-chain amino group and a side-chain carboxyl group. .sup.h) 1,2-amino alcohol residue attached to the C-terminal amino acid residue of module A, involving an amide bond between the α-carboxyl group of the C-terminal amino acid residue and the amino group of the amino alcohol residue, and α-hydroxy acid residue attached to the N-terminal amino acid residue of module A, involving an amide bond between the carboxyl group of the hydroxy acid residue and the α-amino group of the N-terminal amino acid residue. .sup.i) Disulfide interstrand linkage between the indicated amino acid residue and the indicated acid residue in module A, involving a disulfide bond between a pair of side-chain thiol groups as specified. or a pharmaceutically acceptable salt thereof.

    16. A pharmaceutical composition containing a compound or a mixture of compounds according to any one of claims 1 to 15 and at least one pharmaceutically inert carrier.

    17. A pharmaceutical composition according to claim 16 in a form suitable for oral, topical, transdermal, injection, buccal, transmucosal, rectal, pulmonary or inhalation administration, especially in the form of tablets, dragees, capsules, solutions, liquids, gels, plaster, creams, ointments, syrup, slurries, suspensions, spray, nebulizer or suppositories.

    18. Compounds of formula (I) according to any one of claims 1 to 15, or pharmaceutically acceptable salts thereof, for use as a medicament.

    19. Compounds according to any one of the claims 1 to 15 for use as pharmaceutically active substances having antibiotic activity.

    20. The use of compounds according to any one of claims 1 to 15 for the manufacture of a medicament to treat or prevent infections or diseases related to such infections; particularly infections related to respiratory diseases or skin or soft tissue diseases or gastrointestinal diseases or eye diseases or ear diseases or CNS diseases or bone diseases or cardiovascular diseases or genitourinary diseases, or nosocomial infections, or catheter-related and non-catheter-related infections, or urinary tract infections, or bloodstream infections; or infection-induced sepsis; or as a disinfectants or preservatives for foodstuffs, cosmetics, medicaments and other nutrient-containing materials.

    21. The use of compounds according to any one of claims 1 to 15 as pharmaceutically active substances having antibiotic activity.

    22. The use of compounds according to any one of claims 1 to 15, or a composition according to claim 16 or 17, for the treatment or prevention of infections or diseases related to such infections; particularly infections related to respiratory diseases or skin or soft tissue diseases or gastrointestinal diseases or eye diseases or ear diseases or CNS diseases or bone diseases or cardiovascular diseases or genitourinary diseases, or nosocomial infections, or catheter-related and non-catheter-related infections, or urinary tract infections, or bloodstream infections; or infection-induced sepsis; or as a disinfectants or preservatives for foodstuffs, cosmetics, medicaments and other nutrient-containing materials.

    23. A method of treating an infection, especially infections such as nosocomial infections, catheter-related and non-catheter-related infections, urinary tract infections, bloodstream infections, or a disease or disorder associated with an infection, especially diseases or disorders such as ventilator-associated pneumonia (VAP), ventilator-associated bacterial pneumonia (VABP), hospital-acquired pneumonia (HAP), hospital-acquired bacterial pneumonia (HABP), healthcare-associated pneumonia (HCAP), cystic fibrosis, emphysema, asthma, pneumonia, epidemic diarrhea, necrotizing enterocolitis, typhlitis, gastroenteritis, pancreatitis, keratitis, endophthalmitis, otitis, brain abscess, meningitis, encephalitis, osteochondritis, pericarditis, epididymitis, prostatitis, urethritis, sepsis; surgical wounds, traumatic wounds, burns, comprising administering to a subject in need thereof a pharmaceutically acceptable amount of a compound or compounds or a pharmaceutical composition according to any one of claims 1 to 17.

    24. A process for the preparation of compounds according to any one of claims 1 to 15 which comprises process steps being (I) generating a fully protected peptide fragment (module B and linker L) comprising amino acid residues of module B and linker L, as defined above, if coupling to the solid support of the amino acid residue at position Q.sup.7 of module B, as defined above, is via a hydroxyl group of said amino acid residue, by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position Q.sup.7 of module B, as defined above, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (b) removing the N-protecting group from the product obtained in step (a); (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product corresponds to Q.sup.6, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions Q.sup.5 to Q.sup.1, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) if desired or required, selectively removing an N-protecting group at position Q.sup.1 and a carboxyl-protecting group at position Q.sup.7; and generating a macrolactam cycle, as defined above, by formation of an amide bond between the thus liberated carboxyl group at position Q.sup.7 and the amino group at Q.sup.1 of module B; (g) if L is present (k=1, 2, or 3), as defined above, effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions L.sup.k to L.sup.1, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; and, if desired or required, following the coupling, selectively removing an N-protecting group at position Q.sup.1 and a carboxyl-protecting group at position Q.sup.7; and generating a macrolactam cycle, as defined above, by formation of an amide bond between the thus liberated carboxyl group at position Q.sup.7 and the amino group at Q.sup.1 of module B; (h) if L is present and if desired, removing an N-protecting group at position L.sup.1; (i) if L is not present and if desired, removing an N-protecting group at position Q.sup.1; (j) detaching the product thus obtained from the solid support; (k) if desired, selectively protecting the thus liberated hydroxyl group at position Q.sup.7; (l) if L is present, and required, removing an N-protecting group at position L.sup.1; and (m) if L is not present, and required, removing an N-protecting group at position Q.sup.1; if coupling to the solid support of the amino acid residue at position Q.sup.7 of module B, as defined above, is via a carboxyl group of said amino acid residue, by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position Q.sup.7 of module B, as defined above, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (b) removing the N-protecting group from the product obtained in step (a); (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product corresponds to Q.sup.6, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions Q.sup.5 to Q.sup.1, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) if L is present (k=1, 2, or 3), as defined above, effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions L.sup.k to L.sup.1, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (g) if desired, selectively removing an N-protecting group at position Q.sup.1; (h) detaching the product thus obtained from the solid support; (i) if desired and required, selectively removing an N-protecting group at position Q.sup.1; (j) generating a macrolactam cycle, as defined above, by formation of an amide bond between the liberated carboxyl group at position Q.sup.7 and the amino group at Q.sup.1 of module B; (k) if L is present, removing an N-protecting group at position L.sup.1; and (l) if L is not present, removing an N-protecting group at position Q.sup.1; (II) generating a peptide (module A, module B and linker L) comprising residues of module A, module B and linker L, as defined above, if s=1, t=1, and u=1; by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid or, if desired, an appropriately N-protected derivative of that amino alcohol, which in the desired end-product is at position X.sup.13 of module A, as defined above, any functional group which may be present in said N-protected amino acid derivative or N-protected amino alcohol derivative being likewise appropriately protected; (b) removing the N-protecting group from the product thus obtained; (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position X.sup.12, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.11 to P.sup.n (n=5, 6, or 7), any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) selectively removing a carboxyl-protecting group at P.sup.n (n=5, 6, or 7); and coupling of the protected peptide fragment (module B and linker L) by formation of an amide bond between the free amino function in the peptide fragment obtained from procedure (I) and the liberated carboxyl function at P.sup.n; (g) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.n−1 (n=5, 6, or 7) to P.sup.1, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; and, if desired, following coupling of the amino acid, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (h) further effecting steps substantially corresponding to steps (b) to (d) using an appropriately N-protected derivative of an amino acid, or if desired, an appropriately protected derivative of an acid, which in the desired end-product is at position X.sup.14, any functional group(s) which may be present in said N-protected amino acid derivative or acid derivative, being likewise appropriately protected; and, if desired, following the coupling, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (i) if desired, selectively removing the N-protecting group at position X.sup.14, and chemically transforming the thus obtained amino function; (j) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule; (k) detaching the product thus obtained from the solid support; (l) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule to form, for example, an interstrand linkage(s), as defined above; (m) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (n) removing any protecting groups present on functional groups of any members of the chain of residues and, if desired, any protecting group(s) which may in addition be present in the molecule; (o) if desired, implementing additional chemical transformations of one or more reactive group(s) present in the molecule; (p) if desired and required, implementing additional chemical transformations of two or more group(s) present in the molecule to form an interstrand linkage(s), as defined above; and (q) if desired, converting the product thus obtained into a pharmaceutically acceptable salt or converting a pharmaceutically acceptable, or unacceptable, salt thus obtained into the corresponding free compound of formula (I) or into a different, pharmaceutically acceptable salt; if s=1, t=0, and u=1; by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid or, if required, an appropriately N-protected derivative of that amino alcohol, which in the desired end-product is at position X.sup.12 of module A, as defined above, any functional group which may be present in said N-protected amino acid derivative or N-protected amino alcohol derivative being likewise appropriately protected; (b) removing the N-protecting group from the product thus obtained; (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position P.sup.11, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.10 to P.sup.n (n=5, 6, or 7), any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) selectively removing a carboxyl-protecting group at P.sup.n (n=5, 6, or 7); and coupling of the protected peptide fragment (module B and linker L) by formation of an amide bond between the free amino function in the peptide fragment obtained from procedure (I) and the liberated carboxyl function at P.sup.n; (g) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.n−1 (n=5, 6, or 7) to P.sup.1, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; and, if desired, following coupling of the amino acid, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (h) further effecting steps substantially corresponding to steps (b) to (d) using an appropriately N-protected derivative of an amino acid, or if desired, an appropriately protected derivative of an acid, which in the desired end-product is at position X.sup.14, any functional group(s) which may be present in said N-protected amino acid derivative or acid derivative, being likewise appropriately protected; and, if desired, following the coupling, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (i) if desired, selectively removing the N-protecting group at position X.sup.14, and chemically transforming the thus obtained amino function; (j) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule; (k) detaching the product thus obtained from the solid support; (l) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule to form, for example, an interstrand linkage(s), as defined above; (m) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (n) removing any protecting groups present on functional groups of any members of the chain of residues and, if desired, any protecting group(s) which may in addition be present in the molecule; (o) if desired, implementing additional chemical transformations of one or more reactive group(s) present in the molecule; (p) if desired and required, implementing additional chemical transformations of two or more group(s) present in the molecule to form an interstrand linkage(s), as defined above; and (q) if desired, converting the product thus obtained into a pharmaceutically acceptable salt or converting a pharmaceutically acceptable, or unacceptable, salt thus obtained into the corresponding free compound of formula (I) or into a different, pharmaceutically acceptable salt; if s=1, t=1, and u=0; by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid or, if desired, an appropriately N-protected derivative of that amino alcohol, which in the desired end-product is at position X.sup.13 of module A, as defined above, any functional group which may be present in said N-protected amino acid derivative or N-protected amino alcohol derivative being likewise appropriately protected; (b) removing the N-protecting group from the product thus obtained; (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position X.sup.12, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.11 to P.sup.n (n=5, 6, or 7), any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) selectively removing a carboxyl-protecting group at P.sup.n (n=5, 6, or 7); and coupling of the protected peptide fragment (module B and linker L) by formation of an amide bond between the free amino function in the peptide fragment obtained from procedure (I) and the liberated carboxyl function at P.sup.n; (g) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.n−1 (n=5, 6, or 7) to P.sup.2, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; and, if desired, following coupling of the amino acid, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (h) further effecting steps substantially corresponding to steps (b) to (d) using an appropriately N-protected derivative of an amino acid, or if desired, an appropriately protected derivative of a hydroxy acid, or if desired, an appropriately protected derivative of an acid, which in the desired end-product is at position P.sup.1, any functional group(s) which may be present in said N-protected amino acid derivative, hydroxy acid derivative, or acid derivative, being likewise appropriately protected; and, if desired, following the coupling, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (i) if desired, selectively removing the N-protecting group at position P.sup.1, and chemically transforming the thus obtained amino function; (j) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule; (k) detaching the product thus obtained from the solid support; (l) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule to form, for example, an interstrand linkage(s), as defined above; (m) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (n) removing any protecting groups present on functional groups of any members of the chain of residues and, if desired, any protecting group(s) which may in addition be present in the molecule; (o) if desired, implementing additional chemical transformations of one or more reactive group(s) present in the molecule; (p) if desired and required, implementing additional chemical transformations of two or more group(s) present in the molecule to form an interstrand linkage(s), as defined above; and (q) if desired, converting the product thus obtained into a pharmaceutically acceptable salt or converting a pharmaceutically acceptable, or unacceptable, salt thus obtained into the corresponding free compound of formula (I) or into a different, pharmaceutically acceptable salt; if s=0, t=0, and u=1; by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid, which in the desired end-product is at position P.sup.11 of module A, as defined above, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (b) removing the N-protecting group from the product thus obtained; (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position P.sup.10, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.9 to P.sup.n (n=5, 6, or 7), any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) selectively removing a carboxyl-protecting group at P.sup.n (n=5, 6, or 7); and coupling of the protected peptide fragment (module B and linker L) by formation of an amide bond between the free amino function in the peptide fragment obtained from procedure (I) and the liberated carboxyl function at P.sup.n; (g) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.n−1 (n=5, 6, or 7) to P.sup.1, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; and, if desired, following coupling of the amino acid, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (h) further effecting steps substantially corresponding to steps (b) to (d) using an appropriately N-protected derivative of an amino acid, or if desired, an appropriately protected derivative of an acid which in the desired end-product is at position X.sup.14, any functional group(s) which may be present in said N-protected amino acid derivative or acid derivative, being likewise appropriately protected; and, if desired, following the coupling, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (i) if desired, selectively removing the N-protecting group at position X.sup.14, and chemically transforming the thus obtained amino function; (j) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule; (k) detaching the product thus obtained from the solid support; (l) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule to form, for example, an interstrand linkage(s), as defined above; (m) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (n) removing any protecting groups present on functional groups of any members of the chain of residues and, if desired, any protecting group(s) which may in addition be present in the molecule; (o) if desired, implementing additional chemical transformations of one or more reactive group(s) present in the molecule; (p) if desired and required, implementing additional chemical transformations of two or more group(s) present in the molecule to form an interstrand linkage(s), as defined above; and (q) if desired, converting the product thus obtained into a pharmaceutically acceptable salt or converting a pharmaceutically acceptable, or unacceptable, salt thus obtained into the corresponding free compound of formula (I) or into a different, pharmaceutically acceptable salt; if s=1, t=0, and u=0; by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid or, if desired, an appropriately N-protected derivative of that amino alcohol, which in the desired end-product is at position X.sup.12 of module A, as defined above, any functional group which may be present in said N-protected amino acid derivative or N-protected amino alcohol derivative being likewise appropriately protected; (b) removing the N-protecting group from the product thus obtained; (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position P.sup.11, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.10 to P.sup.n (n=5, 6, or 7), any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) selectively removing a carboxyl-protecting group at P.sup.n (n=5, 6, or 7); and coupling of the protected peptide fragment (module B and linker L) by formation of an amide bond between the free amino function in the peptide fragment obtained from procedure (I) and the liberated carboxyl function at P.sup.n; (g) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.n−1 (n=5, 6, or 7) to P.sup.2, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; and, if desired, following coupling of the amino acid, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (h) further effecting steps substantially corresponding to steps (b) to (d) using an appropriately N-protected derivative of an amino acid, or if desired, an appropriately protected derivative of a hydroxy acid, or if desired, an appropriately protected derivative of an acid, which in the desired end-product is at position P.sup.1, any functional group(s) which may be present in said N-protected amino acid derivative, hydroxy acid derivative, or acid derivative, being likewise appropriately protected; and, if desired, following the coupling, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (i) if desired, selectively removing the N-protecting group at position P.sup.1, and chemically transforming the thus obtained amino function; (j) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule; (k) detaching the product thus obtained from the solid support; (l) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule to form, for example, an interstrand linkage(s), as defined above; (m) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (n) removing any protecting groups present on functional groups of any members of the chain of residues and, if desired, any protecting group(s) which may in addition be present in the molecule; (o) if desired, implementing additional chemical transformations of one or more reactive group(s) present in the molecule; (p) if desired and required, implementing additional chemical transformations of two or more group(s) present in the molecule to form an interstrand linkage(s), as defined above; and (q) if desired, converting the product thus obtained into a pharmaceutically acceptable salt or converting a pharmaceutically acceptable, or unacceptable, salt thus obtained into the corresponding free compound of formula (I) or into a different, pharmaceutically acceptable salt; if s=0, t=0, and u=0; and P.sup.11 is not connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position P.sup.11 of module A, as defined above, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (b) removing the N-protecting group from the product thus obtained; (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position P.sup.10, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.9 to P.sup.n (n=5, 6, or 7), any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) selectively removing a carboxyl-protecting group at P.sup.n (n=5, 6, or 7); and coupling of the protected peptide fragment (module B and linker L) by formation of an amide bond between the free amino function in the peptide fragment obtained from procedure (I) and the liberated carboxyl function at P.sup.n; (g) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.n−1 (n=5, 6, or 7) to P.sup.2, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; and, if desired, following coupling of the amino acid, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (h) further effecting steps substantially corresponding to steps (b) to (d) using an appropriately N-protected derivative of an amino acid, or if desired, an appropriately protected derivative of a hydroxy acid, or if desired, an appropriately protected derivative of an acid, which in the desired end-product is at position P.sup.1, any functional group(s) which may be present in said N-protected amino acid derivative, hydroxy acid derivative, or acid derivative, being likewise appropriately protected; and, if desired, following the coupling, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (i) if desired, selectively removing the N-protecting group at position P.sup.1, and chemically transforming the thus obtained amino function; (j) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule; (k) detaching the product thus obtained from the solid support; (l) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule to form, for example, an interstrand linkage(s), as defined above; (m) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and chemically transforming the reactive group(s) thus liberated to form an interstrand linkage(s), as defined above; (n) removing any protecting groups present on functional groups of any members of the chain of residues and, if desired, any protecting group(s) which may in addition be present in the molecule; (o) if desired, implementing additional chemical transformations of one or more reactive group(s) present in the molecule; (p) if desired and required, implementing additional chemical transformations of two or more group(s) present in the molecule to form an interstrand linkage(s), as defined above; and (q) if desired, converting the product thus obtained into a pharmaceutically acceptable salt or converting a pharmaceutically acceptable, or unacceptable, salt thus obtained into the corresponding free compound of formula (I) or into a different, pharmaceutically acceptable salt; if s=0, t=0, and u=0; and P.sup.11 is connected from the α-carbonyl point of attachment to the ω-nitrogen (N) of P.sup.2; by performing steps comprising: (a) coupling an appropriately functionalized solid support with an appropriately N-protected derivative of that amino acid, which in the desired end-product is at position P.sup.11 of module A, as defined above, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (b) removing the N-protecting group from the product thus obtained; (c) coupling the product thus obtained with an appropriately N-protected derivative of that amino acid which in the desired end-product is at position P.sup.10, any functional group which may be present in said N-protected amino acid derivative being likewise appropriately protected; (d) if desired, selectively deprotecting one or several protected functional group(s) present in the molecule and appropriately substituting the reactive group(s) thus liberated by attaching one or several moieties derived from acids, amino acids or amines; (e) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.9 to P.sup.n (n=5, 6, or 7), any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (f) selectively removing a carboxyl-protecting group at P.sup.n (n=5, 6, or 7); and coupling of the protected peptide fragment (module B and linker L) by formation of an amide bond between the free amino function in the peptide fragment obtained from procedure (I) and the liberated carboxyl function at P.sup.n; (g) further effecting steps substantially corresponding to steps (b) to (d) using appropriately N-protected derivatives of amino acids which in the desired end-product are at positions P.sup.n−1 (n=5, 6, or 7) to P.sup.2, any functional group(s) which may be present in said N-protected amino acid derivatives being likewise appropriately protected; (h) further effecting steps substantially corresponding to steps (b) to (d) using an appropriately N-protected derivative of an amino acid, or if desired, an appropriately protected derivative of a hydroxy acid, or if desired, an appropriately protected derivative of an acid, which in the desired end-product is at position P.sup.1, any functional group(s) which may be present in said N-protected amino acid derivative, hydroxy acid derivative, or acid derivative, being likewise appropriately protected; (i) if desired, selectively removing the N-protecting group at position P.sup.1, and chemically transforming the thus obtained amino function; (j) if desired, implementing additional chemical transformations of one or more group(s) present in the molecule; (k) if desired, selectively removing an N-protecting group at position P.sup.2; (l) detaching the product thus obtained from the solid support; (m) if desired, formation of an interstrand linkage, as defined above, by formation of an amide bond between the thus liberated carboxyl group at position P.sup.11 and the amino group at position P.sup.2; (n) if desired and required, selectively removing an N-protecting group at position P.sup.2; and formation of an interstrand linkage, as defined above, by formation of an amide bond between the carboxyl group at position P.sup.11 and the thus liberated amino group at position P.sup.2; (o) removing any protecting groups present on functional groups of any members of the chain of residues and, if desired, any protecting group(s) which may in addition be present in the molecule; (p) if desired, implementing additional chemical transformations of one or more reactive group(s) present in the molecule; and (q) if desired, converting the product thus obtained into a pharmaceutically acceptable salt or converting a pharmaceutically acceptable, or unacceptable, salt thus obtained into the corresponding free compound of formula (I) or into a different, pharmaceutically acceptable salt.

    Description

    EXAMPLES

    [2712] 1. Peptide Synthesis

    [2713] 1.1 Synthetic Procedures

    [2714] A method for the synthesis of the peptidomimetics of the present invention is exemplified in the following. This is to demonstrate the principal concept and does not limit or restrict the present invention in any way. A person skilled in the art is easily able to modify these procedures, especially, but not limited to, choosing a different strategy for formation of a disulfide interstrand linkage and a different fragment coupling strategy, to still achieve the preparation of the claimed cyclic peptidomimetic compounds of the present invention.

    [2715] 1.1.1 Coupling of the First Protected Residue to the Resin

    [2716] 1.1.1.1 Coupling of an Fmoc-Protected Amino Acid to the Resin Via a Side Chain Hydroxyl Group

    [2717] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1% crosslinked; loading: 1.4 mMol/g) was swollen in dry 1,2 dichloroethane for 30 min (4.5 mL 1,2 dichloroethane per g resin). A suspension of 3.2 eq of the Fmoc-protected amino acid and 2 eq of NMM in dry 1,2-dichloroethane (10 mL per g resin) was added. After stirring under reflux for 1-2 h the resin was filtered off and washed with 1,2 dichloroethane (3×) and with CH.sub.2Cl.sub.2. Then a solution of dry CH.sub.2Cl.sub.2/MeOH/DIPEA (17:2:1, v/v/v) was added (10 mL per g resin). After shaking for 3×30 min the resin was filtered off in a pre-weighed sintered funnel and washed successively with CH.sub.2Cl.sub.2, DMF, CH.sub.2Cl.sub.2, MeOH, CH.sub.2Cl.sub.2, MeOH, CH.sub.2Cl.sub.2 (2×) and Et.sub.2O (2×). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.

    [2718] Loading was typically 0.2-0.3 mMol/g.

    [2719] The following preloaded resin was prepared: Fmoc-Thr(-2-chlorotrityl resin)-allyl.

    [2720] 1.1.1.2 Coupling of an Fmoc-Protected Amino Alcohol to the Resin Via a Hydroxyl Group

    [2721] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1% crosslinked; loading: 1.4 mMol/g) was swollen in dry 1,2 dichloroethane for 30 min (4.5 mL 1,2 dichloroethane per g resin). A suspension of 3.2 eq of the Fmoc-protected amino alcohol and 2 eq of NMM in dry 1,2-dichloroethane (10 mL per g resin) was added. After stirring under reflux for 1-2 h the resin was filtered off and washed with 1,2 dichloroethane (3×) and with CH.sub.2Cl.sub.2. Then a solution of dry CH.sub.2Cl.sub.2/MeOH/DIPEA (17:2:1, v/v/v) was added (10 mL per g resin). After shaking for 3×30 min the resin was filtered off in a pre-weighed sintered funnel and washed successively with CH.sub.2Cl.sub.2, DMF, CH.sub.2Cl.sub.2, MeOH, CH.sub.2Cl.sub.2, MeOH, CH.sub.2Cl.sub.2 (2×) and Et.sub.2O (2×). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.

    [2722] Loading was typically 0.2-0.3 mMol/g.

    [2723] The following preloaded resins were prepared: Fmoc-Glyol-2-chlorotrityl resin, Fmoc-Serol(tBu)-2-chlorotrityl resin, Fmoc-Throl(tBu)-2-chlorotrityl resin, Fmoc-.sup.DThrol(tBu)-2-chlorotrityl resin, and Fmoc-Tyrol(tBu)-2-chlorotrityl resin.

    [2724] 1.1.1.3 Coupling of an Fmoc-Protected Amino Acid to the Resin Via a Carboxyl Group

    [2725] In a dried flask, 2-chlorotritylchloride resin (polystyrene, 1% crosslinked; loading: 1.4 mMol/g) was swollen in dry CH.sub.2Cl.sub.2 for 30 min (7 mL CH.sub.2Cl.sub.2 per g resin). A solution of 0.8 eq of the Fmoc-protected amino acid and 6 eq of DIPEA in dry CH.sub.2Cl.sub.2/DMF (4/1, v/v) (10 mL per g resin) was added. After shaking for 2-4 h at rt the resin was filtered off and washed successively with CH.sub.2Cl.sub.2, DMF, CH.sub.2Cl.sub.2, DMF and CH.sub.2Cl.sub.2. Then a solution of dry CH.sub.2Cl.sub.2/MeOH/DIPEA (17:2:1, v/v/v) was added (10 mL per g resin). After shaking for 3×30 min the resin was filtered off in a pre-weighed sintered funnel and washed successively with CH.sub.2Cl.sub.2, DMF, CH.sub.2Cl.sub.2, MeOH, CH.sub.2Cl.sub.2, MeOH, CH.sub.2Cl.sub.2 (2×) and Et.sub.2O (2×). The resin was dried under high vacuum overnight. The final mass of resin was calculated before the qualitative control.

    [2726] Loading was typically 0.6-0.7 mMol/g.

    [2727] The following preloaded resins were prepared: Fmoc-.sup.DAla-2-chlorotrityl resin, Fmoc-.sup.DAsn(Trityl)-2-chlorotrityl resin, Fmoc-Cys(Trityl)-2-chlorotrityl resin, Fmoc-.sup.DDab(Boc)-2-chlorotrityl resin, Fmoc-.sup.DGln(Trityl)-2-chlorotrityl resin, Fmoc-.sup.DGlu(tBu)-2-chlorotrityl resin, Fmoc-.sup.DHse(tBu)-2-chlorotrityl resin, Fmoc-Leu(3R)OtBu-2-chlorotrityl resin, Fmoc-.sup.DLys(Boc)-2-chlorotrityl resin, Fmoc-Ser(tBu)-2-chlorotrityl resin, Fmoc-.sup.DSer(tBu)-2-chlorotrityl resin, Fmoc-Thr(tBu)-2-chlorotrityl resin, Fmoc-.sup.DThr(tBu)-2-chlorotrityl resin, Fmoc-.sup.DVal-2-chlorotrityl resin and Fmoc-.sup.DTyr(tBu)-2-chlorotrityl resin.

    [2728] 1.1.2 Methods for Synthesis on Solid Support of the Fully Protected Peptide and of the Fully Protected Peptide Fragment for Fragment Coupling

    [2729] The synthesis was carried out on a Syro-peptide synthesizer (MultiSynTech GmbH) using 24 to 96 reaction vessels. Unless otherwise indicated, in each vessel were placed 0.05 mMol of the resin, obtained from procedures 1.1.1.1, 1.1.1.2, or 1.1.1.3, as described above, or 0.05 mMol of Sieber amide resin, as described below, and the resin was swelled in CH.sub.2Cl.sub.2 and DMF for 15 min, respectively.

    [2730] The following reaction cycles were programmed and carried out as described in the methods A-K, as described herein below:

    TABLE-US-00001 Step Reagent Time 1 CH.sub.2Cl.sub.2, wash and 1 × 3 min swell (manual) 2 DMF, wash and swell 2 × 30 min 3 20% piperidine/DMF 1 × 5 min and 1 × 15 min 4 DMF, wash 5 × 1 min   5 .sup.a) 3.6 eq appropriately protected 1 × 40 min amino acid and 3.6 eq HOAt in DMF or NMP + 3.6 eq DIC in DMF 6 3.6 eq appropriately protected 1 × 40 min amino acid and 3.6 eq HOAt in DMF or NMP + 3.6 eq HATU + 7.2 eq DIPEA in NMP 7 DMF, wash 5 × 1 min 8 20% piperidine/DMF 1 × 5 min and 1 × 15 min or 2 × 2 min .sup.b) 9 DMF, wash 5 × 1 min 10  CH.sub.2Cl.sub.2, wash (at the end of 3 × 1 min the synthesis) .sup.a) In the coupling cycle following coupling of an N-alkyl amino acid residue and for coupling of the first protected amino acid residue to Sieber amide resin, step 5 was omitted and step 6 was performed twice instead. .sup.b) Reduced times were used for Fmoc deprotection of an amino acid residue having a carboxyl group protected as allyl ester, and for the Fmoc deprotection step of the following coupling cycle.

    [2731] The term “macrolactam cycle”, as used herein below, refers to a cyclic peptide moiety that is generated through formation of an amide bond between two amino acid residues of module B, involving an α-carboxyl group and a side-chain amino group.

    [2732] The term “lactam interstrand linkage”, as used herein, refers to a linkage of two amino acid residues of module A by an amide bond, involving a side-chain carboxyl group and a side-chain amino group; or, an α-carboxyl group and a side-chain amino group.

    [2733] 1.1.2.1 Method A

    [2734] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide fragment (module B and linker L) using 0.05 mMol of the resin obtained from procedure 1.1.1.1 and appropriately protected Fmoc amino acid building blocks.

    [2735] In a first part, a fully protected peptide fragment encompassing amino acid residues of module B was prepared. Steps 5 to 9 are repeated to add each amino acid residue of module B, except for the last amino acid residue of this peptide fragment, which was added by steps 5 to 7. Subsequently, allyl and alloc deprotection (module B) and macrolactam cycle formation (module B) were performed as described in the corresponding section of procedure A herein below, followed by steps 8 to 9 for Fmoc deprotection and washing.

    [2736] Assembly of the fully protected peptide fragment was then continued. Steps 5 to 9 were repeated to add each amino acid residue of linker L.

    [2737] 1.1.2.2 Method B

    [2738] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of the resin obtained from procedure 1.1.1.2 and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L) and the last coupling, as described herein below. For the latter, an appropriately protected Boc-amino acid building block was used.

    [2739] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2740] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A, except for the last amino acid residue, which was added by steps 5 to 7, followed by step 10.

    [2741] 1.1.2.3 Method C

    [2742] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of the resin obtained from procedure 1.1.1.2 and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L), as described herein below.

    [2743] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with amino acid residue at position L.sup.1 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed. Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A.

    [2744] 1.1.2.4 Method D

    [2745] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of the resin obtained from procedure 1.1.1.2 and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L) and the last coupling, as described herein below. For the latter, an acid building block was used.

    [2746] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with amino acid residue at position L.sup.1 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2747] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A, except for the acid residue, which was added by steps 5 to 7, followed by step 10.

    [2748] 1.1.2.5 Method E

    [2749] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of the resin obtained from procedure 1.1.1.2 and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L) and the last coupling, as described herein below. For the latter, an appropriately protected hydroxy acid building block was used.

    [2750] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2751] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A, except for the hydroxy acid residue, which was added by steps 5 to 7, followed by step 10.

    [2752] 1.1.2.6 Method F

    [2753] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of the resin obtained from procedure 1.1.1.3 and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L) and the last coupling, as described herein below. For the latter, an appropriately protected Boc-amino acid building block was used.

    [2754] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2755] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A, except for the last amino acid residue, which was added by steps 5 to 7, followed by step 10.

    [2756] 1.1.2.7 Method G

    [2757] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of the resin obtained from procedure 1.1.1.3 and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L), as described herein below.

    [2758] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2759] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A.

    [2760] 1.1.2.8 Method H

    [2761] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of the resin obtained from procedure 1.1.1.3 and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L) and the last coupling, as described herein below. For the latter, an appropriately protected hydroxy acid building block was used.

    [2762] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding section of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2763] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A, except for the hydroxy acid residue, which was added by steps 5 to 7, followed by step 10.

    [2764] 1.1.2.9 Method I

    [2765] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of Sieber amide resin (polystyrene, 1% crosslinked; loading: 0.65 mMol/g) and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L), and the last coupling, as described herein below. For the latter, an appropriately protected Boc-amino acid building block was used.

    [2766] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2767] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A, except for the last amino acid residue, which was added by steps 5 to 7, followed by step 10.

    [2768] 1.1.2.10 Method J

    [2769] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of Sieber amide resin (polystyrene, 1% crosslinked; loading: 0.65 mMol/g) and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L), as described herein below.

    [2770] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2771] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A.

    [2772] 1.1.2.11 Method K

    [2773] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of Sieber amide resin (polystyrene, 1% crosslinked; loading: 0.65 mMol/g) and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L) and the last coupling, as described herein below. For the latter, an appropriately protected hydroxy acid building block was used. In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2774] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A, except for the hydroxy acid residue, which was added by steps 5 to 7, followed by step 10.

    [2775] 1.1.2.12 Method L

    [2776] The reaction cycles, as described herein above, were applied for the assembly of the fully protected peptide (module A, module B and linker L), using 0.05 mMol of Sieber amide resin (polystyrene, 1% crosslinked; loading: 0.65 mMol/g) and appropriately protected Fmoc amino acid building blocks, except for coupling of the protected peptide fragment (module B and linker L) and the last coupling, as described herein below. For the latter, an acid building block was used.

    [2777] In a first part, steps 5 to 9 are repeated to add each amino acid residue of module A, except for the case, where the carboxyl group-bearing side chain of the added amino acid residue of module A is connected with the amino acid residue at position 12 of linker L. In this case, coupling of the allyl protected Fmoc amino acid by steps 5 to 7 was followed by allyl deprotection and coupling of the protected peptide fragment (module B and linker L) as described in the corresponding sections of procedure A herein below. Subsequently, steps 8 to 9 for Fmoc protection and washing were performed.

    [2778] Assembly of the fully protected peptide was then continued. Steps 5 to 9 were repeated to add each remaining amino acid residue of module A, except for the acid residue, which was added by steps 5 to 7, followed by step 10.

    [2779] 1.1.3 Procedures for the Preparation of the Peptides

    [2780] One of the procedures A Q, as described herein below, was adopted for preparation of the peptides.

    [2781] 1.1.3.1 Procedure A:

    [2782] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having an Amino Alcohol Residue Attached to the C-Terminal Amino Acid Residue and Having a Free N-Terminal Amino Group

    [2783] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2784] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2785] The appropriately protected peptide fragment encompassing amino acid residues of module B and linker L was assembled on solid support according to Method A as described above. Allyl and alloc deprotection, and macrolactam cycle formation were performed as follows:

    [2786] Allyl and Alloc Deprotection (Module B)

    [2787] For selective removal of the allyl and alloc protecting groups from carboxyl and amino functions present in the resin bound peptide, the latter (0.05 mMol) was swollen in 1 mL dry CH.sub.2Cl.sub.2 for at least 10 min, washed twice with iPrOH and twice with iPr.sub.2O, followed by addition of 40 eq triphenylsilane in 0.5 mL NMP, shaking of the mixture for 1 minute, and addition of 0.2 eq tetrakis(triphenylphosphine)palladium(0) in 0.5 mL dry CH.sub.2Cl.sub.2. After shaking the reaction mixture for 5 min at rt, the resin was filtered off and washed three times with 1 mL dry CH.sub.2Cl.sub.2. The deprotection procedure was repeated with fresh solutions of reagents, applying a shaking time of 15 min after addition of the palladium catalyst. LC-MS was used to monitor the deprotection reaction and, if required, the deprotection procedure was repeated. Subsequently the resin was thoroughly washed with CH.sub.2Cl.sub.2, DMF, iPrOH, and finally again with CH.sub.2Cl.sub.2.

    [2788] Macrolactam Cycle Formation (Module B)

    [2789] 1 eq OxymaPure in 0.4 mL CH.sub.2Cl.sub.2 and 2 eq DIC in 0.6 mL CH.sub.2Cl.sub.2 were added to the resin in CH.sub.2Cl.sub.2. After stirring the reaction mixture for approximately 2-3 h, the resin was filtered, and fresh solutions of reagents were added to repeat the procedure. The resin was subsequently filtered and washed with CH.sub.2Cl.sub.2, DMF, iPrOH, and finally again with CH.sub.2Cl.sub.2.

    [2790] Subsequently the following steps were performed:

    [2791] Cleavage of Peptide Fragment from Resin (Module B and Linker L)

    [2792] The resin was swollen in 1 mL CH.sub.2Cl.sub.2 (2×10 min). After filtration, the resin was suspended in 1 mL of 1% TFA in CH.sub.2Cl.sub.2 (v/v) for 5 min. The resin was then filtered and washed three times with 1 mL of CH.sub.2Cl.sub.2, and a solution of 1 mL of 40% DIPEA in CH.sub.2Cl.sub.2 (v/v) was added to the combined filtrate and washings. The cleavage procedure was repeated 6 times. LC-MS was used to monitor the cleavage and, if required, the cleavage procedure was repeated further.

    [2793] The combined filtrate and washings were evaporated to dryness.

    [2794] Preparation of Free Base Peptide Fragment (Module B and Linker L)

    [2795] The obtained protected peptide fragment was then dissolved in 4 mL of MeOH/CH.sub.2Cl.sub.2 (1:4, v/v) and washed twice with 2 mL of aq. Na.sub.2CO.sub.3 (0.1 M). The organic layer was dried (Na.sub.2SO.sub.4), filtered, and evaporated to dryness.

    [2796] (II) Preparation of the Peptide (Module A, Module B and Linker L)

    [2797] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method B as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as follows:

    [2798] Allyl Deprotection

    [2799] Selective removal of the allyl protecting group from a carboxyl function was performed as described in the corresponding section above for allyl and alloc deprotection (module B).

    [2800] Coupling of Protected Peptide Fragment (Module B and Linker L)

    [2801] The resin was swollen in 1 mL DMF for 10 min and then filtered off. The swelling procedure was repeated once with fresh DMF. Subsequently, 1 eq OxymaPure in 0.4 mL CH.sub.2Cl.sub.2/DMSO (1:1, v/v) and 2 eq DIC in 0.6 mL CH.sub.2Cl.sub.2 were added to the resin in DMF. After stirring the reaction mixture for approximately 5-10 minutes, 1.2 eq protected peptide fragment (module B and linker L) in 0.5 mL CH.sub.2Cl.sub.2/DMSO (1:1, v/v) were added. The reaction mixture was then stirred for approximately 16 h. Afterwards, the resin was filtered and washed three times with CH.sub.2Cl.sub.2/DMSO (1:1, v/v), and finally with DMF.

    [2802] Subsequently, cleavage of the peptide from the resin and disulfide bridge formation were performed as follows:

    [2803] Cleavage of Peptide from Resin

    [2804] The resin was swollen in 1 mL CH.sub.2Cl.sub.2 (2×10 min). After filtration, the resin was suspended in 1 mL of 1% TFA in CH.sub.2Cl.sub.2 (v/v) for 5 min. The resin was then filtered and washed three times with 1 mL of CH.sub.2Cl.sub.2, and a solution of 1 mL of 40% DIPEA in CH.sub.2Cl.sub.2 (v/v) was added to the combined filtrate and washings. The cleavage procedure was repeated 6 times. LC-MS was used to monitor the cleavage and, if required, the cleavage procedure was repeated further.

    [2805] The combined filtrate and washings were evaporated to dryness.

    [2806] Formation of Disulfide Interstrand Linkage(s) (Module A)

    [2807] The protected peptide was dissolved in 8 mL of HFIP/CH.sub.2Cl.sub.2 (1:4, v/v) and 2 eq iodine in 2 mL of HFIP/CH.sub.2Cl.sub.2 (1:4, v/v) were added. After shaking for 20-45 minutes, 3 mL of a 1 M aqueous solution of ascorbic acid were added to quench excess reagent, and the mixture was further shaken for 10 min. The aqueous phase was discarded, optionally applying a centrifugation step for phase separation. The organic phase was washed with 4 mL of H.sub.2O, and concentrated to dryness.

    [2808] Full Deprotection

    [2809] To fully deprotect the peptide, 7 mL of cleavage cocktail TFA/TIS/H.sub.2O (95:2.5:2.5, v/v/v) were added, and the mixture was kept for 2.5-4 h at room temperature. The reaction mixture was evaporated close to dryness, the peptide precipitated with 7 mL of cold Et.sub.2O/pentane (1:1, v/v) and finally washed three times with 3 mL of cold Et.sub.2O/pentane (1:1, v/v).

    [2810] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2811] 1.1.3.2 Procedure B

    [2812] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having an Amino Alcohol Residue Attached to the C-Terminal Amino Acid Residue and being Acylated at the N-Terminal Amino Group

    [2813] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2814] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2815] The appropriately protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2816] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2817] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method C as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2818] Acylation of the N-terminal amino group was then carried out as follows:

    [2819] Acylation

    [2820] After assembly of the peptide on the resin, steps 5 to 7 of the programmed reaction cycles were performed using 3.6 eq appropriate acid instead of 3.6 eq protected amino acid, followed by step 10.

    [2821] Subsequently, cleavage of the peptide from the resin, formation of a disulfide interstrand linkage(s), and full deprotection were performed as indicated in the corresponding sections of procedure A, following the same order.

    [2822] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2823] 1.1.3.3 Procedure C

    [2824] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having an Amino Alcohol Residue Attached to the C-Terminal Amino Acid Residue and Having an Acid Residue Attached to the N-Terminal Amino Acid Residue

    [2825] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2826] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2827] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2828] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2829] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method D as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2830] Subsequently, cleavage of the peptide from the resin, formation of a disulfide interstrand linkage(s), and full deprotection were performed as indicated in the corresponding sections of procedure A, following the same order.

    [2831] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2832] 1.1.3.4 Procedure D:

    [2833] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module a Having an Amino Alcohol Residue Attached to the C-Terminal Amino Acid Residue and Having an α-Hydroxy Acid Residue Attached to the N-Terminal Amino Acid Residue

    [2834] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2835] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2836] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2837] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2838] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method E as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2839] Subsequently, cleavage of the peptide from the resin, formation of a disulfide interstrand linkage(s), and full deprotection were performed as indicated in the corresponding sections of procedure A, following the same order.

    [2840] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2841] 1.1.3.5 Procedure E:

    [2842] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having a Free C-Terminal Carboxyl Group and Having a Free N-Terminal Amino Group

    [2843] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2844] (I) Preparation of a protected peptide fragment (module B and linker L)

    [2845] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2846] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2847] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method F as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2848] Subsequently, cleavage of the peptide from the resin, formation of a disulfide interstrand linkage(s), and full deprotection were performed as indicated in the corresponding sections of procedure A, following the same order.

    [2849] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2850] 1.1.3.6 Procedure F:

    [2851] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module a Having a Free C-Terminal Carboxyl Group and being Acylated at the N-Terminal Amino Group

    [2852] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2853] (I) Preparation of a Protected Peptide Fragment (Module 13 and Linker L)

    [2854] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2855] (II) Preparation of a Peptide (Module a, Module 13 and Linker L)

    [2856] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method G as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2857] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [2858] Subsequently, cleavage of the peptide from the resin, formation of a disulfide interstrand linkage(s), and full deprotection were performed as indicated in the corresponding sections of procedure A, following the same order.

    [2859] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2860] 1.1.3.7 Procedure G

    [2861] Preparation of a Peptide Having a Lactam Interstrand Linkage Between a Side-Chain Carboxyl Group and a Side-Chain Amino Group in Module a Having a Free C-Terminal Carboxyl Group and Having a Free N-Terminal Amino Group

    [2862] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2863] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2864] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2865] (II Preparation of a Peptide (Module a, Module B and Linker L)

    [2866] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method F as described above. Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2867] Subsequently, the following steps were performed:

    [2868] Allyl Deprotection

    [2869] Selective removal of the allyl protecting group from the carboxyl function was performed as described in the corresponding section for allyl and alloc deprotection (module B) in procedure A.

    [2870] ivDde Deprotection

    [2871] The resin was swollen in 1 mL DMF for 10 min and subsequently filtered off. For deprotection, 1 mL of a 5% solution of hydrazine monohydrate in DMF (v/v) was added and the reaction mixture was shaken for 30 min. The reaction mixture was then filtered off and washed with 1 mL DMF. The deprotection step was repeated by employing the same amount of reagents. LC-MS was used to monitor the deprotection reaction and, if required, the deprotection procedure was repeated again. Finally, the resin was thoroughly washed with DMF, CH.sub.2Cl.sub.2, DMF, and iPrOH, and finally washed with CH.sub.2Cl.sub.2.

    [2872] Formation of Lactam Interstrand Linkage

    [2873] To the resin swollen in CH.sub.2Cl.sub.2, 2 eq FDPP in 0.5 mL DMF and 2 eq DIPEA in 0.5 mL CH.sub.2Cl.sub.2 were added. After stirring the reaction mixture for approximately 16 h at rt, the resin was filtered off, and fresh solutions of reagents were added to repeat the procedure. Subsequently, the resin was washed three times with DMF.

    [2874] Cleavage of peptide from resin and full deprotection were then performed as indicated in the corresponding sections of procedure A.

    [2875] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below

    [2876] 1.1.3.8 Procedure H:

    [2877] Preparation of a Peptide Having a Disulfide Interstrand Linkage in Module A Having a Carboxy Methylamide Group at the C-Terminus and being Acylated at the N-Terminal Amino Group

    [2878] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2879] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2880] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2881] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2882] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method G as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2883] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B. Subsequently, cleavage of the peptide from the resin was performed as indicated in the corresponding section of procedure A.

    [2884] Afterwards the following step was performed:

    [2885] Formation of the Carboxy Methylamide Group

    [2886] The protected peptide was solubilized in 0.5 mL CH.sub.2Cl.sub.2, followed by the addition of 1 mL DMF and of 4 eq. CH.sub.3NH.sub.2 (100 μl, 2M CH.sub.3NH.sub.2 in THF). Then 2 eq NMM in 2 mL DMF, and 2 eq HATU and 1 eq HOAt in 2 mL DMF were added, and the reaction mixture was stirred for approximately 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 mL of CH.sub.2Cl.sub.2 and washed three times with 4.5 mL 10% acetonitrile in water (v/v). The CH.sub.2Cl.sub.2 layer was then evaporated to dryness.

    [2887] Subsequently, formation of a disulfide interstrand linkage(s) and full deprotection were performed as indicated in the corresponding sections of procedure A.

    [2888] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below

    [2889] 1.1.3.9 Procedure I:

    [2890] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A

    [2891] Having a Carboxyisopropyl Ester Group at the C-Terminus and being Acylated at the N-Terminal Amino Group

    [2892] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2893] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2894] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2895] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2896] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method G as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2897] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [2898] Subsequently, the following step was performed:

    [2899] Cleavage of Peptide from Resin and Formation of the Carboxyisopropyl Ester Group

    [2900] The resin (0.05 mMol) was swollen in 1 mL CH.sub.2Cl.sub.2 (2×10 min). To the resin in 0.6 mL CH.sub.2Cl.sub.2, 108 eq. acetyl chloride (1.8 mL, freshly prepared solution of 3M acetyl chloride in iPrOH at 0° C.) were added. After shaking the reaction mixture for 24 hours, the resin was filtered off and washed with three times 1 ml CH.sub.2Cl.sub.2, and the combined filtrate and washings were evaporated to dryness.

    [2901] Subsequently, full deprotection and formation of a disulfide interstrand linkage(s) were performed as indicated in the corresponding sections of procedure M2.

    [2902] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2903] 1.1.3.10 Procedure J:

    [2904] Preparation of a Peptide Having a Lactam Interstrand Linkage Between a Side-Chain Amino Group and the C-Terminal Carboxyl Group in Module A and being Acylated at the N-Terminal Amino Group

    [2905] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2906] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2907] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2908] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2909] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method G as described above. Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2910] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [2911] Subsequently, removal of the alloc protecting group from the amino function and cleavage of the peptide from the resin, in this order, were performed as described for allyl and alloc deprotection (module B), and cleavage of peptide from resin in the corresponding sections of procedure A.

    [2912] Formation of a lactam interstrand linkage was then carried out as follows:

    [2913] Lactam Interstrand Linkage Formation

    [2914] The protected peptide was first solubilized in 0.5 mL CH.sub.2Cl.sub.2, followed by the addition of 8 mL DMF. Then 6 eq NMM in 2 mL DMF, and 2 eq HATU and 1 eq HOAt in 2 mL DMF were added, and the reaction mixture was stirred for approximately 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 mL of CH.sub.2Cl.sub.2 and washed three times with 4.5 mL 10% acetonitrile in water (v/v). The CH.sub.2Cl.sub.2 layer was then evaporated to dryness.

    [2915] Full deprotection was afterwards performed as indicated in the corresponding section of procedure A.

    [2916] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2917] 1.1.3.11 Procedure K:

    [2918] Preparation of a Peptide Having a Lactam Interstrand Linkage Between a Side-Chain Amino Group and the C-Terminal Carboxyl Group in Module A and Having an α-Hydroxy Acid at the N-Terminus

    [2919] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2920] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2921] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2922] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2923] The fully protected peptide fragment was assembled on solid support according to Method H as described above. Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2924] Subsequently, removal of the alloc protecting group from the amino function, cleavage of the peptide from the resin, formation of a lactam interstrand linkage, and full deprotection, in this order, were then performed as indicated in procedure J.

    [2925] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2926] 1.1.3.12 Procedure L:

    [2927] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having a Carboxylamide Group at the C-Terminus and Having a Free N-Terminal Amino Group

    [2928] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2929] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2930] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2931] (II) Preparation of a Peptide (Module A, Module B and Linker L)

    [2932] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method I as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2933] Subsequently, cleavage of the peptide from the resin was carried out as follows:

    [2934] Cleavage of Peptide from Resin

    [2935] The resin was swollen in 1 mL CH.sub.2Cl.sub.2 (2×10 min). After filtration, the resin was suspended in 1 mL of 1% TFA in CH.sub.2Cl.sub.2 (v/v) for 10-30 min. The resin was then filtered and washed three times with 1 mL of CH.sub.2Cl.sub.2, and a solution of 1 mL of 40% DIPEA in CH.sub.2Cl.sub.2 (v/v) was added to the combined filtrate and washings. LC-MS was used to monitor the cleavage and, if required, the cleavage procedure was repeated 3-5 times. The combined filtrate and washings were evaporated to dryness.

    [2936] Formation of a disulfide interstrand linkage(s) and full deprotection were performed as indicated in the corresponding sections of procedure A.

    [2937] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2938] 1.1.3.13 Procedure M1:

    [2939] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having a Carboxylamide Group at the C-Terminus and being Acylated at the N-Terminal Amino Group

    [2940] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2941] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2942] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2943] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2944] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method J as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2945] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [2946] Subsequently, cleavage of the peptide from the resin, formation of a disulfide interstrand linkage(s), and full deprotection were performed as indicated in the corresponding sections of procedure L, following the same order.

    [2947] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2948] 1.1.3.14 Procedure M2:

    [2949] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having a Carboxylamide Group at the C-Terminus and being Acylated at the N-Terminal Amino Group

    [2950] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2951] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2952] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2953] (I) Preparation of a Peptide (Module a, Module B and Linker L)

    [2954] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method J as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2955] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [2956] Subsequently, cleavage of the peptide from the resin was performed as indicated in the corresponding section of procedure L.

    [2957] Afterwards full deprotection and formation of a disulfide interstrand linkage(s) were performed as follows:

    [2958] Full Deprotection

    [2959] To fully deprotect the peptide, 7 mL of cleavage cocktail TFA/TIS/thioanisole/anisole/water (82.5:2.5:5:5:5, v/v/v/v/v) were added, and the mixture was kept for 2.5-4 h at room temperature. The reaction mixture was evaporated close to dryness, the peptide precipitated with 7 mL of cold Et.sub.2O/pentane (1:1, v/v) and finally washed 3 times with 4 mL of cold Et.sub.2O/pentane.

    [2960] Formation of a Disulfide Interstrand Linkage(s)

    [2961] The deprotected peptide was dissolved in 0.8 mL DMSO, 7.2 mL aq. NH.sub.4OAc (0.5 M, adjusted to pH 8 with aq. NH.sub.4OH (28% in water, w/v)) were added, and the reaction mixture was then stirred for 24 h at rt. LC-MS was used to monitor the formation of the disulfide interstrand linkages and, if required, the reaction mixture was stirred for further 24 h at rt, followed again by LC-MS monitoring.

    [2962] Thereafter, the reaction mixture was adjusted to pH 5-6 by addition of acetic acid and evaporated to dryness.

    [2963] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2964] 1.1.3.15 Procedure N1:

    [2965] Preparation of a Peptide Having a Lactam Interstrand Linkage Between a Side-Chain Carboxyl Group and a Side-Chain Amino Group in Module a Having a Carboxylamide Group at the C-Terminus and being Acylated at the N-Terminal Amino Group

    [2966] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2967] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2968] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2969] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2970] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method J as described above. Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2971] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [2972] Subsequently, removal of the alloc protecting group from the amino function was performed as described for allyl and alloc deprotection (module B) in the corresponding section of procedure A.

    [2973] Thereafter, the following steps was carried out:

    [2974] Cleavage of Peptide from Resin and Removal of the 2-Phenyl-Isopropyl Protecting Group from the Carboxyl Function

    [2975] The resin was swollen in 1 mL CH.sub.2Cl.sub.2 (2×10 min). After filtration, the resin was suspended in 1 mL of 1% TFA in CH.sub.2Cl.sub.2 (v/v) for 10-30 min. The resin was then filtered and washed three times with 1 mL of CH.sub.2Cl.sub.2, and a solution of 1 mL of 40% DIPEA in CH.sub.2Cl.sub.2 (v/v) was added to the combined filtrate and washings. LC-MS was used to monitor the cleavage and, if required, the cleavage procedure was repeated 3-5 times. The combined filtrate and washings were evaporated to dryness.

    [2976] Lactam Interstrand Linkage Formation

    [2977] The protected peptide was first solubilized in 0.5 mL CH.sub.2Cl.sub.2, followed by the addition of 8 mL DMF. Then 6 eq NMM in 2 mL DMF, and 2 eq HATU and 1 eq HOAt in 2 mL DMF were added, and the reaction mixture was stirred for approximately 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 mL of CH.sub.2Cl.sub.2 and washed three times with 4.5 mL 10% acetonitrile in water (v/v). The CH.sub.2Cl.sub.2 layer was then evaporated to dryness.

    [2978] Full deprotection was then performed as indicated in the corresponding section of procedure A.

    [2979] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2980] 1.1.3.16 Procedure N2:

    [2981] Preparation of a Peptide Having a Lactam Interstrand Linkage Between a Side-Chain Carboxyl Group and a Side-Chain Amino Group in Module A Having a Carboxylamide Group at the C-Terminus and being Acylated at the N-Terminal Amino Group

    [2982] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2983] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2984] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2985] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2986] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method J as described above. Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [2987] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [2988] Subsequently, the following step was performed:

    [2989] ivDde Deprotection

    [2990] The resin was swollen in 1 mL DMF for 10 min and subsequently filtered off. For deprotection, 1 mL of a 5% solution of hydrazine monohydrate in DMF (v/v) was added and the reaction mixture was shaken for 30 min. The reaction mixture was then filtered off and washed with 1 mL DMF. The deprotection step was repeated by employing the same amount of reagents. LC-MS was used to monitor the deprotection reaction and, if required, the deprotection procedure was repeated again. Finally, the resin was thoroughly washed with DMF, CH.sub.2Cl.sub.2, DMF, and iPrOH, and finally washed again with CH.sub.2Cl.sub.2.

    [2991] Cleavage of peptide from resin and removal of the 2-phenyl-isopropyl protecting group from the carboxyl function, formation of the lactam interstrand linkage and full deprotection were then performed as indicated in the corresponding section of procedure N1, in the same order.

    [2992] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [2993] 1.1.3.17 Procedure O:

    [2994] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having a Carboxylamide Group at the C-Terminus and Having an α-Hydroxy Acid Residue Attached to the N-Terminal Amino Acid Residue

    [2995] The peptide was prepared based on an on-resin fragment coupling strategy.

    [2996] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [2997] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [2998] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [2999] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method K as described above. Appropriately protected Fmoc amino acid building blocks with a thiol group protected as trityl thioether were used for the addition of amino acid residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [3000] Subsequently, cleavage of the peptide from the resin, formation of a disulfide interstrand linkage(s), and full deprotection were performed as indicated in the corresponding sections of procedure L, following the same order.

    [3001] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [3002] 1.1.3.18 Procedure P:

    [3003] Preparation of a Peptide Having a Disulfide Interstrand Linkage(s) in Module A Having a Carboxylamide Group at the C-Terminus and Having a Thiol-Substituted Acid Residue Attached to the N-Terminal Amino Acid Residue

    [3004] The peptide was prepared based on an on-resin fragment coupling strategy.

    [3005] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [3006] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [3007] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [3008] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method L as described above. An appropriately protected Fmoc amino acid building block(s) with a thiol group protected as trityl thioether and an appropriately protected acid building block with a thiol group protected as trityl thioether were used for the addition of the residues that are involved in the formation of a disulfide interstrand linkage(s). Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [3009] Subsequently, cleavage of the peptide from the resin, formation of a disulfide interstrand linkage(s), and full deprotection were performed as indicated in the corresponding sections of procedure L, following the same order.

    [3010] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [3011] 1.1.3.19 Procedure Q:

    [3012] Preparation of a Peptide Having a Salt Bridge(s) in Module A Having a Carboxylamide Group at the C-Terminus and being Acylated at the N-Terminal Amino Group

    [3013] The peptide was prepared based on an on-resin fragment coupling strategy.

    [3014] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [3015] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [3016] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [3017] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method J as described above. Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [3018] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [3019] Subsequently, cleavage of the peptide from the resin and full deprotection were performed as indicated in the corresponding sections of procedure L.

    [3020] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [3021] 1.1.3.20 Procedure R:

    [3022] Preparation of a Peptide Having a Lactam Interstrand Linkage Between a Side-Chain Carboxyl Group and a Side-Chain Amino Group in Module A Having a Carboxylamide Group at the C-Terminus and being Acetylated at the N-Terminal Amino Group

    [3023] The peptide was prepared based on an on-resin fragment coupling strategy.

    [3024] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [3025] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [3026] (II Preparation of a Peptide (Module a, Module B and Linker L)

    [3027] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method J as described above. Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [3028] Acylation of the N-terminal amino group was then carried out as indicated in the corresponding section of procedure B.

    [3029] Subsequently, allyl-deprotection, ivDde deprotection, and formation of lactam interstrand linkage were performed as indicated in the corresponding section of procedure G, following the same order.

    [3030] Cleavage of peptide from resin and full deprotection were then performed as indicated in the corresponding sections of procedure A.

    [3031] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [3032] 1.1.3.21 Procedure S:

    [3033] Preparation of a Peptide Having a Lactam Interstrand Linkage Between a Side-Chain Carboxyl Group and a Side-Chain Amino Group in Module A Having a Carboxylamide Group at the C-Terminus and Having an α-Hydroxy Acid at the N-Terminus

    [3034] The peptide was prepared based on an on-resin fragment coupling strategy.

    [3035] (I) Preparation of a Protected Peptide Fragment (Module B and Linker L)

    [3036] The protected peptide fragment encompassing amino acid residues of module B and linker L was prepared as described in the corresponding section of procedure A.

    [3037] (II) Preparation of a Peptide (Module a, Module B and Linker L)

    [3038] The fully protected peptide (module A, module B and linker L) was assembled on solid support according to Method K as described above. Allyl deprotection and coupling of the protected peptide fragment (module B and linker L) were performed as indicated in the corresponding sections of procedure A.

    [3039] Subsequently, removal of the alloc protecting group from the amino function was performed as described for allyl and alloc deprotection (module B) in the corresponding section of procedure A.

    [3040] Thereafter, the following steps was carried out:

    [3041] Cleavage of Peptide from Resin and Removal of the 2-Phenyl-Isopropyl Protecting Group from the Carboxyl Function

    [3042] The resin was swollen in 1 mL CH.sub.2Cl.sub.2 (2×10 min). After filtration, the resin was suspended in 1 mL of 1% TFA in CH.sub.2Cl.sub.2 (v/v) for 10-30 min. The resin was then filtered and washed three times with 1 mL of CH.sub.2Cl.sub.2, and a solution of 1 mL of 40% DIPEA in CH.sub.2Cl.sub.2 (v/v) was added to the combined filtrate and washings. LC-MS was used to monitor the cleavage and, if required, the cleavage procedure was repeated 3-5 times. The combined filtrate and washings were evaporated to dryness.

    [3043] Lactam Interstrand Linkage Formation

    [3044] The protected peptide was first solubilized in 0.5 mL CH.sub.2Cl.sub.2, followed by the addition of 8 mL DMF. Then 6 eq NMM in 2 mL DMF, and 2 eq HATU and 1 eq HOAt in 2 mL DMF were added, and the reaction mixture was stirred for approximately 16 h. The volatiles were removed by evaporation. The crude cyclic peptide was dissolved in 7 mL of CH.sub.2Cl.sub.2 and washed three times with 4.5 mL 10% acetonitrile in water (v/v). The CH.sub.2Cl.sub.2 layer was then evaporated to dryness.

    [3045] Full deprotection was then performed as indicated in the corresponding section of procedure A.

    [3046] Finally, the peptide was purified by preparative reverse phase LC-MS, as described herein below.

    [3047] 1.1.4 Purification Procedure (Preparative Reverse Phase LC-MS)

    [3048] Compounds were purified by reverse phase chromatography using a Waters XBridge C8 OBD column, 30×150 mm, 5 μm (Cat No. 186003083), a Waters XSelect C18 OBD column, 30×150 mm, 5 μm (Cat. 186005426), or a Waters CSH XSelect Phenyl Hexyl column, 50×300 mm, 5 μm.

    [3049] Mobile phases used were:

    [3050] A: 0.1% TFA in Water/Acetonitrile 98/2 v/v

    [3051] B: 0.1% TFA in Acetonitrile

    [3052] Gradient slopes in the preparative runs were adapted each time based on analytical LC-MS analysis of the crude product. As an example, a typical run (purification of Ex. 204) was executed using two Waters CSH XSelect Phenyl Hexyl columns in series with a flow rate of 130 mL/min and at a column temperature of 50° C., running a gradient from 0-2.1 min 0% B, at 2.2 min 14% B to 38.2 min 18% B, and finally 48.0-55.0 min 100% B (retention time: 20.7 min in this case).

    [3053] Detection: MS and UV @ 220 nm

    [3054] Fractions collected were evaporated using a Genevac HT4/HT12 evaporator or a Buchi system.

    [3055] Alternatively for larger amounts the following LC-purification system was used:

    [3056] Column: Waters XBridge C18 OBD column, 50×250 mm, 10 μm (Cat No. 186003900)

    [3057] Mobile phase A: 0.1% TFA in Water/Acetonitrile 98/2 v/v

    [3058] Mobile phase B: 0.1% TFA in Acetonitrile

    [3059] Flow rate: 150 mL/min

    [3060] Detection: UV @ 220 nm

    [3061] After lyophilisation the products were obtained typically as white to off-white powders. Unless otherwise indicated the obtained products as TFA salts were analysed by HPLC-ESI-MS methods as described below. Salt exchange to obtain the corresponding products as acetate salts or chloride salts was performed using procedures described under 1.1.5, and obtained products as acetate salts or chloride salts were analysed by HPLC-ESI-MS methods as described below.

    [3062] 1.1.5 Salt Exchange Procedure

    [3063] Purification of compounds according to procedure 1.1.4 above provided the products as TFA salts. Conversion of the products to the corresponding acetate salts was performed using AG® 1-X2 Resin (acetate form, 2% crosslinkage, 200-400 dry mesh size; Bio-Rad, 140-1253). For the conversion of the products to the corresponding chloride salts AG® 1-X2 Resin (chloride form, 2% crosslinkage, 200-400 dry mesh; Bio-Rad, 140-1251) was used. Salt exchanges were carried out based on the corresponding instruction manual of the supplier.

    [3064] After lyophilisation the products were obtained typically as white to off-white powders and analysed by HPLC-ESI-MS methods as described below.

    [3065] 1.2 Analytical Methods

    [3066] 1.2.1 Analytical Method A

    [3067] Analytical HPLC retention times (rt, in minutes) were determined using an Ascentis Express C8 column 100×3 mm, 2.7 μm (Supelco, 53852-U) with the following solvents A (H.sub.2O+0.1% TFA) and B (CH.sub.3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 7 min: 45% A, 55% B; 7.02-7.5 min: 3% A, 97% B; 7.52-7.8 min: 95% A, 5% B. Flow rate=1.4 mL/min at 55° C.

    [3068] 1.2.2 Analytical Method B

    [3069] Analytical HPLC retention times (rt, in minutes) were determined using a Poroshell Bonus RP 100×3 mm, 2.7 μm (Agilent technologies, 695968-301) with the following solvents A (H.sub.2O+0.1% TFA) and B (CH.sub.3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 7 min: 45% A, 55% B; 7.02-7.5 min: 3% A, 97% B; 7.52-7.8 min: 95% A, 5% B. Flow rate=1.4 mL/min at 55° C.

    [3070] 1.2.3 Analytical Method C

    [3071] Analytical HPLC retention times (rt, in minutes) were determined using an Ascentis Express C8 column, 100×3 mm, 2.7 μm (Supelco, 53852-U) with the following solvents A (H.sub.2O+0.1% TFA) and B (CH.sub.3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 7 min: 15% A, 85% B; 7.02-7.5 min: 3% A, 97% B; 7.52-7.8 min: 95% A, 5% B. Flow rate=1.4 mL/min at 55° C.

    [3072] 1.2.4 Analytical Method D

    [3073] Analytical HPLC retention times (rt, in minutes) were determined using an Ascentis Express C8 column 100×3 mm, 2.7 μm (Supelco, 53852-U) with the following solvents A (H.sub.2O+0.1% TFA) and B (CH.sub.3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 7 min: 45% A, 55% B; 7.02-7.5 min: 3% A, 97% B; 7.52-7.8 min: 95% A, 5% B. Flow rate=1.4 mL/min at 70° C.

    [3074] 1.2.5 Analytical Method E

    [3075] Analytical HPLC retention times (rt, in minutes) were determined using an Ascentis Express C8 column 100×3 mm, 2.7 μm (Supelco, 53852-U) with the following solvents A (H.sub.2O+0.1% TFA) and B (CH.sub.3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 11 min: 45% A, 55% B; 11.02-12.5 min: 3% A, 97% B; 12.55-13.5 min: 95% A, 5% B. Flow rate=1.4 mL/min at 55° C.

    [3076] 1.2.6 Analytical Method F

    [3077] Analytical HPLC retention times (rt, in minutes) were determined using a Poroshell Bonus RP 100×3 mm, 2.7 μm (Agilent technologies, 695968-301) with the following solvents A (H.sub.2O+0.1% TFA) and B (CH.sub.3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 7 min: 45% A, 55% B; 7.02-7.5 min: 3% A, 97% B; 7.52-7.8 min: 95% A, 5% B. Flow rate=1.4 mL/min at 70° C.

    [3078] 1.2.7 Analytical Method G

    [3079] Analytical HPLC retention times (rt, in minutes) were determined using a XSelect CSH Phenyl-Hexyl 150×3 mm, 2.5 μm (Waters, 186006734) with the following solvents A (H2O 2O+0.1% TFA) and B (CH3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 7 min: 45% A, 55% B; 7.02-7.7 min: 3% A, 97% B; 7.72-9.95 min: 95% A, 5% B. Flow rate=1.3 mL/min at 55° C.

    [3080] 1.2.8 Analytical Method H

    [3081] Analytical HPLC retention times (rt, in minutes) were determined using a Ascentis Express C8 100×3 mm, 2.7 μm (Supelco, 53852-U) with the following solvents A (H2O 2O+0.1% TFA) and B (CH3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 12.1 min: 45% A, 55% B; 12.12-13.1 min: 3% A, 97% B; 13.12-14.8 min: 95% A, 5% B. Flow rate=0.750 mL/min at 55° C.

    [3082] 1.2.8 Analytical Method I

    [3083] Analytical HPLC retention times (rt, in minutes) were determined using a Poroshell Bonus RP 100×3 mm, 2.7 μm (Agilent technologies, 695968-301) with the following solvents A (H2O 2O+0.1% TFA) and B (CH3CN+0.085% TFA) and the gradient: 0-0.1 min: 95% A, 5% B; 12.1 min: 45% A, 55% B; 12.12-13.1 min: 3% A, 97% B; 13.12-15.2 min: 95% A, 5% B. Flow rate=0.750 mL/min at 55° C.

    [3084] 1.3 Synthesis of Peptide Sequences

    [3085] Example 1 is shown in Table 1.

    [3086] Procedure C, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3087] (I) The protected peptide fragment (module B and linker L) was synthesized starting with the amino acid Fmoc-Thr-allyl ester, which was grafted to the resin (Fmoc-Thr(-2-chlorotrityl resin)-allyl). The peptide fragment was synthesized on solid support according to method A as described above. Following coupling of Fmoc-Dab(Alloc)-OH for addition of the amino acid residue at Q.sup.1, allyl and alloc deprotection (module B), and macrolactam cycle formation (module B) by an amide bond between the liberated α-carboxyl group of Thr at Q.sup.7 and the liberated γ-amino group of Dab at Q.sup.1 was performed as indicated in the corresponding sections of procedure A above. Assembly of the peptide fragment was in the following sequence:

    [3088] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3089] Subsequently, cleavage of the protected peptide fragment from the resin and preparation of the free base of the protected peptide fragment were performed as indicated in procedure A above.

    [3090] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method D as described above.

    [3091] The peptide was synthesized starting with the amino alcohol Fmoc-Glyol, which was grafted to the resin (Fmoc-Glyol-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at at P.sup.5 and using 3-methyl-butanoic acid for addition of the acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3092] Resin-Glyol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3093] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure C above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 1 in Table 2.

    [3094] Examples 2 and 4 are shown in Table 1.

    [3095] Procedure C, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3096] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1. Assembly of the peptide fragment was in the following sequence:

    [3097] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3098] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method D as described above.

    [3099] The peptides were synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5 and using 3-methyl-butanoic acid for addition of the acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3100] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3101] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure C above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 2 and 4 in Table 2. Example 3 is shown in Table 1.

    [3102] Procedure C, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3103] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1. Assembly of the peptide fragment was in the following sequence:

    [3104] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3105] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method D as described above.

    [3106] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5 and using isobutyric acid for addition of the acid residue at P.sup.1. Coupling of the protected fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3107] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3108] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure C above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 3 in Table 2.

    [3109] Example 5 is shown in Table 1.

    [3110] Procedure C, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3111] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3112] Assembly of the peptide fragment was in the following sequence:

    [3113] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3114] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method D as described above.

    [3115] The peptide was synthesized starting with the amino alcohol Fmoc-Serol(tBu), which was grafted to the resin (Fmoc-Serol(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5 and using 3-methyl-butanoic acid for addition of the acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3116] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3117] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure C above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 5 in Table 2.

    [3118] Examples 6, 8 and 10 are shown in Table 1.

    [3119] Procedure M1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3120] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3121] Assembly of the peptide fragment was in the following sequence:

    [3122] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3123] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J.

    [3124] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at P.sup.11 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3125] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3126] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 6, 8 and 10 in Table 2.

    [3127] Example 7 is shown in Table 1.

    [3128] Procedure O, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3129] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1. Assembly of the peptide fragment was in the following sequence:

    [3130] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1

    [3131] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method K as described above.

    [3132] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at P.sup.11 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3133] Resin-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3134] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 7 in Table 2.

    [3135] Examples 9 and 57 are shown in Table 1.

    [3136] Procedure L, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3137] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3138] Assembly of the peptide fragments was in the following sequence:

    [3139] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3140] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method I as described above.

    [3141] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at P.sup.11 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3142] Resin-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3143] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure L above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 9 and 57 in Table 2.

    [3144] Example 11 is shown in Table 1.

    [3145] Procedure M1, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3146] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3147] Assembly of the peptide fragment was in the following sequence:

    [3148] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3149] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3150] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at P.sup.11 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3151] Resin-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3152] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 11 in Table 2.

    [3153] Example 12 is shown in Table 1.

    [3154] Procedure L, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3155] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1. Assembly of the peptide fragment was in the following sequence:

    [3156] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3157] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method I as described above.

    [3158] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at P.sup.11 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3159] Resin-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3160] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure L above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 12 in Table 2.

    [3161] Examples 13 and 14 are shown in Table 1.

    [3162] Procedure M1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3163] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3164] Assembly of the peptide fragment was in the following sequence:

    [3165] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3166] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J.

    [3167] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at P.sup.10 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3168] Resin-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3169] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 13 and 14 in Table 2.

    [3170] Examples 15 to 18, 23, 25 and 31 to 38 are shown in Table 1.

    [3171] Procedure J, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3172] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1. Assembly of the peptide fragments was in the following sequence:

    [3173] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3174] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method G as described above.

    [3175] The peptides were synthesized starting with the amino acid Fmoc-.sup.DThr(tBu)-OH, which was grafted to the resin (Fmoc-.sup.DThr(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3176] Resin-.sup.DThr-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3177] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptides from the resin, formation of the lactam interstrand linkage by an amide bond between the liberated side-chain amino group of the amino acid residue at P.sup.2 and the liberated α-carboxyl group of .sup.DThr at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 15 to 18, 23, 25 and 31 to 38 in Table 2.

    [3178] Example 19 is shown in Table 1.

    [3179] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3180] (l) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3181] Assembly of the peptide fragment was in the following sequence:

    [3182] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3183] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3184] The peptide was synthesized starting with the amino acid Fmoc-.sup.DAsn(Trityl)-OH, which was grafted to the resin (Fmoc-.sup.DAsn(Trityl)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3185] Resin-.sup.DAsn-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3186] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DAsn at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 19 in Table 2.

    [3187] Example 20 is shown in Table 1.

    [3188] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3189] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3190] Assembly of the peptide fragment was in the following sequence:

    [3191] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3192] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3193] The peptide was synthesized starting with the amino acid Fmoc-.sup.DGln(Trityl)-OH, which was grafted to the resin (Fmoc-.sup.DGln(Trityl)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3194] Resin-.sup.DGln-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3195] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DGln at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 20 in Table 2.

    [3196] Example 21 is shown in Table 1.

    [3197] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3198] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3199] Assembly of the peptide fragment was in the following sequence:

    [3200] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3201] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3202] The peptide was synthesized starting with the amino acid Fmoc-.sup.DGlu(tBu)-OH, which was grafted to the resin (Fmoc-.sup.DGlu(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3203] Resin-.sup.DGlu-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3204] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DGlu at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 21 in Table 2.

    [3205] Example 22 is shown in Table 1.

    [3206] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3207] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3208] Assembly of the peptide fragment was in the following sequence:

    [3209] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3210] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3211] The peptide was synthesized starting with the amino acid Fmoc-.sup.DHse(tBu)-OH, which was grafted to the resin (Fmoc-.sup.DHse(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3212] Resin-.sup.DHse-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3213] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DHse at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 22 in Table 2.

    [3214] Example 24 is shown in Table 1.

    [3215] Procedure K, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3216] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3217] Assembly of the peptide fragment was in the following sequence:

    [3218] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3219] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method H as described above.

    [3220] The peptide was synthesized starting with the amino acid Fmoc-.sup.DThr(tBu)-OH, which was grafted to the resin (Fmoc-.sup.DThr(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3221] Resin-.sup.DThr-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3222] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DThr at P.sup.11, and full deprotection were performed as indicated in procedure K above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 24 in Table 2.

    [3223] Example 26 is shown in Table 1.

    [3224] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3225] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3226] Assembly of the peptide fragment was in the following sequence:

    [3227] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3228] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3229] The peptide was synthesized starting with the amino acid Fmoc-.sup.DTyr(tBu)-OH, which was grafted to the resin (Fmoc-.sup.DTyr(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3230] Resin-.sup.DTyr-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3231] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DTyr at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 26 in Table 2.

    [3232] Example 27 is shown in Table 1.

    [3233] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3234] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3235] Assembly of the peptide fragment was in the following sequence:

    [3236] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3237] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3238] The peptide was synthesized starting with the amino acid Fmoc-.sup.DVal-OH, which was grafted to the resin (Fmoc-.sup.DVal-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3239] Resin-.sup.DVal-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3240] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DVal at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 27 in Table 2.

    [3241] Example 28 is shown in Table 1.

    [3242] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3243] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3244] Assembly of the peptide fragment was in the following sequence:

    [3245] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3246] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3247] The peptide was synthesized starting with the amino acid Fmoc-.sup.DDab(Boc)-OH, which was grafted to the resin (Fmoc-.sup.DDab(Boc)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3248] Resin-.sup.DDab-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3249] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DDab at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 28 in Table 2.

    [3250] Example 29 is shown in Table 1.

    [3251] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3252] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3253] Assembly of the peptide fragment was in the following sequence:

    [3254] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3255] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3256] The peptide was synthesized starting with the amino acid Fmoc-.sup.DOrn(Boc)-OH, which was grafted to the resin (Fmoc-.sup.DOrn(Boc)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3257] Resin-.sup.DOrn-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3P.sup.2-P.sup.1.

    [3258] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DOrn at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 29 in Table 2.

    [3259] Example 30 is shown in Table 1.

    [3260] Procedure J, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3261] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3262] Assembly of the peptide fragment was in the following sequence:

    [3263] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3264] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3265] The peptide was synthesized starting with the amino acid Fmoc-.sup.DLys(Boc)-OH, which was grafted to the resin (Fmoc-.sup.DLys(Boc)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3266] Resin-.sup.DLys-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3267] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptide from the resin, formation of the lactam interstrand linkage by an amide bond between the δ-amino group of Orn at P.sup.2 and the liberated α-carboxyl group of .sup.DLys at P.sup.11, and full deprotection were performed as indicated in procedure J above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 30 in Table 2.

    [3268] Examples 39 to 41, 44 to 46, 49, 62 to 68, 119 and 144 are shown in Table 1.

    [3269] Procedure M1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3270] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3271] Assembly of the peptide fragments was in the following sequence:

    [3272] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3273] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3274] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3275] Resin-X.sup.11-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3276] Subsequently, acylation with acetic acid at P.sup.1 (Ex. 39, 41, 44 to 46, 49, and 62 to 68) or acylation with 6-methly heptanoic acid at P.sup.1 (Ex. 40) or acylation with propionic acid at P.sup.1 (Ex. 119 and 144), cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 39 to 41, 44 to 46, 49, 62 to 68, 119 and 144 in Table 2.

    [3277] Examples 100, 113, 114, 117, 120, 121, 128, 130 to 143, 150 to 156, 158, 159, 251 to 264, 267 to 269, 272, 275, 276, 278, 280 to 284, 289, 294 to 300, 305 to 318, 328 to 339, 342, 343, 345, 350, 352 and 353 are shown in Table 1.

    [3278] Procedure M2, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3279] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3280] Assembly of the peptide fragments was in the following sequence:

    [3281] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3282] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3283] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3284] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3285] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, full deprotection, and formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11 were performed as indicated in procedure M2 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 100, 113, 114, 117, 120, 121, 128, 130 to 143, 150 to 156, 158, 159, 251 to 264, 267 to 269, 272, 275, 276, 278, 280 to 284, 289, 294 to 300, 305 to 318, 328 to 339, 342, 343, 345, 350, 352 and 353 in Table 2.

    [3286] Example 42 is shown in Table 1.

    [3287] Procedure E, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3288] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3289] Assembly of the peptide fragment was in the following sequence:

    [3290] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3291] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method F as described above.

    [3292] The peptide was synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was grafted to the resin (Fmoc-Ser(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3293] Resin-Ser-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3294] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure E above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 42 in Table 2.

    [3295] Examples 43, 47, 48, 50 and 51 are shown in Table 1.

    [3296] Procedure L, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3297] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3298] Assembly of the peptide fragment was in the following sequence:

    [3299] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3300] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method I as described above.

    [3301] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3302] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3303] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure L above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 43, 47, 48, 50 and 51 in Table 2.

    [3304] Example 52 is shown in Table 1.

    [3305] Procedure F, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3306] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3307] Assembly of the peptide fragment was in the following sequence:

    [3308] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3309] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3310] The peptide was synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was grafted to the resin (Fmoc-Ser(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3311] Resin-Ser-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3312] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure F above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 52 in Table 2.

    [3313] Examples 53 and 54 are shown in Table 1.

    [3314] Procedure E, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3315] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3316] Assembly of the peptide fragment was in the following sequence:

    [3317] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3318] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method F as described above.

    [3319] The peptides were synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was grafted to the resin (Fmoc-Ser(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3320] Resin-Ser-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3321] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure E above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 53 and 54 in Table 2.

    [3322] Examples 55 and 56 are shown in Table 1.

    [3323] Procedure G, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3324] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3325] Assembly of the peptide fragment was in the following sequence:

    [3326] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3327] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method F as described above.

    [3328] The peptides were synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was grafted to the resin (Fmoc-Ser(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3329] Resin-Ser-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3330] Subsequently, allyl deprotection at P.sup.2, ivDde deprotection at P.sup.11, and formation of the lactam interstrand linkage by an amide bond between the liberated side-chain functional groups of the amino acid residue at P.sup.2 and Dab at P.sup.11, cleavage of the peptides from the resin, and full deprotection were performed as indicated in procedure G above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 55 and 56 in Table 2.

    [3331] Examples 58, 60, 61, 74 to 76, 78 to 85, 87 to 91 and 104 to 112 are shown in Table 1. Procedure D, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3332] (I) The protected peptide fragments (module B and linker L) were synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3333] Assembly of the peptide fragment was in the following sequence:

    [3334] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3335] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method E as described above.

    [3336] The peptides were synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3337] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3338] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 58, 60, 61, 74 to 76, 78 to 85, 87 to 91 and 104 to 112 in Table 2.

    [3339] Examples 59, 72 and 73 are shown in Table 1.

    [3340] Procedure D, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3341] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3342] Assembly of the peptide fragment was in the following sequence:

    [3343] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3344] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method E as described above.

    [3345] The peptides were synthesized starting with the amino alcohol Fmoc-Glyol, which was grafted to the resin (Fmoc-Glyol-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3346] Resin-Glyol-P.sup.11; P.sup.10; P.sup.9; P.sup.8; P.sup.7; P.sup.6; P.sup.5; P.sup.4; P.sup.3; P.sup.2-Hiv.

    [3347] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 59, 72 and 73 in Table 2.

    [3348] Examples 69 and 70 are shown in Table 1.

    [3349] Procedure D, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3350] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3351] Assembly of the peptide fragment was in the following sequence:

    [3352] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3353] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method E as described above.

    [3354] The peptides were synthesized starting with the amino alcohol Fmoc-Glyol, which was grafted to the resin (Fmoc-Glyol-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3355] Resin-Glyol-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-Hiv.

    [3356] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 69 and 70 in Table 2.

    [3357] Example 71 is shown in Table 1.

    [3358] Procedure B, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3359] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3360] Assembly of the peptide fragment was in the following sequence:

    [3361] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3362] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method C as described above.

    [3363] The peptide was synthesized starting with the amino alcohol Fmoc-Glyol, which was grafted to the resin (Fmoc-Glyol-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3364] Resin-Glyol-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3365] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure B above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 71 in Table 2.

    [3366] Example 77 is shown in Table 1.

    [3367] Procedure A, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3368] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3369] Assembly of the peptide fragment was in the following sequence:

    [3370] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3371] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method B as described above.

    [3372] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3373] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3374] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure A above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 77 in Table 2.

    [3375] Examples 86, 123 and 129 are shown in Table 1.

    [3376] Procedure B, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3377] (I) The protected peptide fragments (module B and linker L) were synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3378] Assembly of the peptide fragments was in the following sequence:

    [3379] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3380] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method C as described above.

    [3381] The peptides were synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3382] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3383] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure B above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 86, 123 and 129 in Table 2.

    [3384] Examples 92 and 93 are shown in Table 1.

    [3385] Procedure D, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3386] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3387] Assembly of the peptide fragment was in the following sequence:

    [3388] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3389] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method E as described above.

    [3390] The peptides were synthesized starting with the amino alcohol Fmoc-Tyrol(tBu), which was grafted to the resin (Fmoc-Tyrol(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3391] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3392] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 92 and 93 in Table 2.

    [3393] Example 94 is shown in Table 1.

    [3394] Procedure B, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3395] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3396] Assembly of the peptide fragment was in the following sequence:

    [3397] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3398] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method C as described above.

    [3399] The peptide was synthesized starting with the amino alcohol Fmoc-Tyrol(tBu), which was grafted to the resin (Fmoc-Tyrol(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3400] Resin-Tyrol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3401] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure B above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 94 in Table 2.

    [3402] Examples 95, 97 and 101 to 103 are shown in Table 1.

    [3403] Procedure D, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3404] (I) The protected peptide fragments (module B and linker L) were synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3405] Assembly of the peptide fragments were in the following sequence:

    [3406] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3407] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method E as described above.

    [3408] The peptides were synthesized starting with the amino alcohol Fmoc-Serol(tBu), which was grafted to the resin (Fmoc-Serol(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3409] Resin-Serol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3410] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 95, 97 and 101 to 103 in Table 2.

    [3411] Examples 96, 98 and 116 are shown in Table 1.

    [3412] Procedure B, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3413] (I) The protected peptide fragments (module B and linker L) were synthesized as indicated above in the corresponding section in the synthesis of Ex. 1. Assembly of the peptide fragments was in the following sequence:

    [3414] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3415] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method C as described above.

    [3416] The peptides were synthesized starting with the amino alcohol Fmoc-Serol(tBu), which was grafted to the resin (Fmoc-Serol(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3417] Resin-Serol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3418] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure B above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 96, 98 and 116 in Table 2.

    [3419] Example 99, 115, 157, 270, 271, 274, 277, 301, 340, and 344 are shown in Table 1. Procedure O, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3420] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3421] Assembly of the peptide fragment was in the following sequence:

    [3422] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3423] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method K as described above.

    [3424] The peptides were synthesized starting with an appropriately protected Fmoc amino acid which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3425] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3426] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 99, 115, 157, 270, 271, 274, 277, 301, 340, and 344 in Table 2.

    [3427] Example 122 is shown in Table 1.

    [3428] Procedure I, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3429] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3430] Assembly of the peptide fragment was in the following sequence:

    [3431] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3432] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3433] The peptide was synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was grafted to the resin (Fmoc-Ser(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3434] Resin-Ser-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3435] Subsequently, cleavage of the peptide from resin and formation of the isopropyl ester of the liberated α-carboxyl group of Ser at X.sup.12, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure I above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 122 in Table 2.

    [3436] Example 124 is shown in Table 1.

    [3437] Procedure B, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3438] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3439] Assembly of the peptide fragment was in the following sequence:

    [3440] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3441] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method C as described above.

    [3442] The peptide was synthesized starting with the amino alcohol Fmoc-.sup.DThrol(tBu), which was grafted to the resin (Fmoc-.sup.DThrol(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3443] Resin-.sup.DThrol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3444] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure B above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 124 in Table 2.

    [3445] Examples 125 and 126 are shown in Table 1.

    [3446] Procedure M1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3447] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3448] Assembly of the peptide fragment was in the following sequence:

    [3449] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3450] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3451] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at P.sup.11 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3452] Resin-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3453] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 125 and 126 in Table 2.

    [3454] Example 127 is shown in Table 1.

    [3455] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3456] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3457] Assembly of the peptide fragment was in the following sequence:

    [3458] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.1.

    [3459] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3460] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3461] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3462] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 127 in Table 2.

    [3463] Example 145 is shown in Table 1.

    [3464] Procedure H, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3465] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3466] Assembly of the peptide fragment was in the following sequence:

    [3467] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3468] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3469] The peptide was synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was grafted to the resin (Fmoc-Ser(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3470] Resin-Ser-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3471] Subsequently, cleavage of the peptide from resin, formation of the N-methlyamide of the liberated α-carboxyl group of Ser at X.sup.12, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure H above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 145 in Table 2.

    [3472] Examples 146 and 147 are shown in Table 1.

    [3473] Procedure N1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3474] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3475] Assembly of the peptides fragment was in the following sequence:

    [3476] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3477] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3478] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-Glu(2-PhiPr)-OH for addition of the amino acid residue at P.sup.11 and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3479] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3480] Subsequently, acylation with acetic acid at P.sup.1, removal of the alloc protecting group at P.sup.2, cleavage of the peptides from resin and removal of the 2-phenyl-isopropyl protecting group at P.sup.11, formation of the lactam interstrand linkage by an amide bond between the liberated side-chain functional groups of the residues at P.sup.2 and at P.sup.11, and full deprotection were performed as indicated in procedure N1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 146 and 147 in Table 2.

    [3481] Examples 148, 149, 265, 273, 279, 287, 290, 291, 293, 302, 303, 319 to 327, 341, 346, 348, 349 and 351 are shown in Table 1.

    [3482] Procedure N1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3483] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3484] Assembly of the peptide fragments was in the following sequence:

    [3485] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3486] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3487] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5 and using Fmoc-Asp(2-PhiPr)-OH for addition of the amino acid residue at P.sup.11. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3488] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3489] Subsequently, acylation with acetic acid at P.sup.1, removal of the alloc protecting group at P.sup.2, cleavage of the peptides from the resin and removal of the 2-phenyl-isopropyl protecting group at P.sup.11, formation of the lactam interstrand linkage by an amide bond between the liberated side-chain functional groups of the residues at P.sup.2 and at P.sup.11, and full deprotection were performed as indicated in procedure N1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 148, 149, 265, 273, 279, 287, 290, 291, 293, 302, 303, 319 to 327, 341, 346, 348, 349 and 351 in Table 2.

    [3490] Example 160 is shown in Table 1.

    [3491] Procedure O, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3492] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3493] Assembly of the peptide fragment was in the following sequence:

    [3494] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3495] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method K as described above.

    [3496] The peptide was synthesized starting with an appropriately protected Fmoc amino acid which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3497] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3498] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 160 in Table 2.

    [3499] Example 161 is shown in Table 1.

    [3500] Procedure O, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3501] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3502] Assembly of the peptide fragment was in the following sequence:

    [3503] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3504] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method K as described above.

    [3505] The peptide was synthesized starting with an appropriately protected Fmoc amino acid which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-.sup.DGlu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of .sup.DGlu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3506] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3507] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 161 in Table 2.

    [3508] Example 162 is shown in Table 1.

    [3509] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3510] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3511] Assembly of the peptide fragment was in the following sequence:

    [3512] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3513] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3514] The peptide was synthesized starting with the amino alcohol Fmoc-Serol(tBu), which was grafted to the resin (Fmoc-Serol(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3515] Resin-Serol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3516] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 162 in Table 2.

    [3517] Example 163 is shown in Table 1.

    [3518] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3519] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3520] Assembly of the peptide fragment was in the following sequence:

    [3521] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3522] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3523] The peptide was synthesized starting with the amino alcohol Fmoc-Serol(tBu), which was grafted to the resin (Fmoc-Serol(tBu)-2-chlorotrityl resin), using Fmoc-.sup.DGlu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of .sup.DGlu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3524] Resin-Serol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3525] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 163 in Table 2.

    [3526] Example 164 is shown in Table 1.

    [3527] Procedure O, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3528] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3529] Assembly of the peptide fragment was in the following sequence:

    [3530] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.1.

    [3531] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method K as described above.

    [3532] The peptide was synthesized starting with an appropriately protected Fmoc amino acid which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3533] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3534] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 164 in Table 2.

    [3535] Example 165 is shown in Table 1.

    [3536] Procedure O, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3537] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3538] Assembly of the peptide fragment was in the following sequence:

    [3539] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.1.

    [3540] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method K as described above.

    [3541] The peptide was synthesized starting with an appropriately protected Fmoc amino acid which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-.sup.DGlu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of .sup.DGlu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence:

    [3542] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3543] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 165 in Table 2.

    [3544] Examples 166, 167 and 168 are shown in Table 1.

    [3545] Procedure O, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3546] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3547] Assembly of the peptide fragment was in the following sequence:

    [3548] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3549] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method K as described above.

    [3550] The peptides were synthesized starting with an appropriately protected Fmoc amino acid which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.7, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.7 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3551] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3552] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 166, 167 and 168 in Table 2.

    [3553] Examples 169, 170 and 171 are shown in Table 1.

    [3554] Procedure O, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3555] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3556] Assembly of the peptide fragment was in the following sequence:

    [3557] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3558] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method K as described above.

    [3559] The peptides were synthesized starting with an appropriately protected Fmoc amino acid which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-.sup.DGlu(Allyl)-OH for addition of the amino acid residue at P.sup.7, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of .sup.DGlu at P.sup.7 and the α-amino group of Dab at C. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3560] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3561] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 169, 170 and 171 in Table 2.

    [3562] Examples 172, 173 and 174 are shown in Table 1.

    [3563] Procedure D, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3564] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3565] Assembly of the peptide fragment was in the following sequence:

    [3566] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3567] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method E as described above.

    [3568] The peptides were synthesized starting with the amino alcohol Fmoc-Serol(tBu), which was grafted to the resin (Fmoc-Serol(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.7, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.7 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3569] Resin-Serol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3570] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure D above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 172, 173 and 174 in Table 2.

    [3571] Example 175 is shown in Table 1.

    [3572] Procedure M1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3573] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3574] Assembly of the peptide fragments was in the following sequence:

    [3575] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1.

    [3576] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3577] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3578] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3579] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, formation of the disulfide interstrand linkages between P.sup.2 and P.sup.11 and between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 175 in Table 2.

    [3580] Examples 176 and 177 are shown in Table 1.

    [3581] Procedure L, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3582] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3583] Assembly of the peptide fragment was in the following sequence:

    [3584] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3585] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method I as described above.

    [3586] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3587] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3588] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkages between P.sup.2 and P.sup.11 and between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure L above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 176 and 177 in Table 2.

    [3589] Examples 178, 179, 205 to 208 and 215 are shown in Table 1.

    [3590] Procedure M1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3591] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3592] Assembly of the peptide fragments was in the following sequence:

    [3593] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3594] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3595] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3596] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3597] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 178, 179, 205 to 208 and 215 in Table 2.

    [3598] Examples 219 to 227 and 266 are shown in Table 1.

    [3599] Procedure M2, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3600] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3601] Assembly of the peptide fragments was in the following sequence:

    [3602] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1

    [3603] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3604] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3605] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3606] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, full deprotection and formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9 were performed as indicated in procedure M2 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 219 to 227 and 266 in Table 2.

    [3607] Examples 180 to 185 are shown in Table 1.

    [3608] Procedure L, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3609] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3610] Assembly of the peptide fragments was in the following sequence:

    [3611] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3612] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method I as described above.

    [3613] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3614] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3615] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure L above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 180 to 185 in Table 2.

    [3616] Example 186 is shown in Table 1.

    [3617] Procedure E, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3618] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3619] Assembly of the peptide fragment was in the following sequence:

    [3620] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1.

    [3621] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method F as described above.

    [3622] The peptide was synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was grafted to the resin (Fmoc-Ser(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3623] Resin-Ser-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3624] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure E above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 186 in Table 2.

    [3625] Example 187 is shown in Table 1.

    [3626] Procedure N2, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3627] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3628] Assembly of the peptide fragment was in the following sequence:

    [3629] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3630] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3631] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at) X.sup.12 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using Fmoc-Asp(2-PhiPr)-OH for addition of the amino acid residue at P.sup.4. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3632] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3633] Subsequently, acylation with acetic acid at P.sup.1, ivDde deprotection at P.sup.9, cleavage of the peptide from the resin and removal of the 2-phenyl-isopropyl protecting group at P.sup.4, formation of a lactam interstrand linkage by an amide bond between the liberated β-carboxyl group of Asp at P.sup.4 and the γ-amino group of Dab at P.sup.9, and full deprotection were performed as indicated in procedure N2 above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 187 in Table 2.

    [3634] Example 188 to 195, 198 to 202 and 204 are shown in Table 1.

    [3635] Procedure D, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3636] (I) The protected peptide fragments (module B and linker L) were synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3637] Assembly of the peptide fragments was in the following sequence:

    [3638] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3639] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method E as described above.

    [3640] The peptides were synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3641] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3642] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 188 to 195, 198 to 202 and 204 in Table 2.

    [3643] Example 196 is shown in Table 1.

    [3644] Procedure B, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3645] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3646] Assembly of the peptide fragment was in the following sequence:

    [3647] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3648] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method C as described above.

    [3649] The peptide was synthesized starting with the amino alcohol Fmoc-Serol(tBu), which was grafted to the resin (Fmoc-Serol(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3650] Resin-Serol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3651] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure B above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 196 in Table 2.

    [3652] Example 197 is shown in Table 1.

    [3653] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3654] (I) The protected peptide fragment (module B and linker L) were synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3655] Assembly of the peptide fragment was in the following sequence:

    [3656] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3657] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3658] The peptide was synthesized starting with the amino alcohol Fmoc-Serol(tBu), which was grafted to the resin (Fmoc-Serol(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3659] Resin-Serol-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-Hiv.

    [3660] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 197 in Table 2.

    [3661] Example 203 is shown in Table 1.

    [3662] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3663] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3664] Assembly of the peptide fragment was in the following sequence:

    [3665] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3666] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3667] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.7, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.7 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3668] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-Hiv.

    [3669] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 203 in Table 2.

    [3670] Example 209 is shown in Table 1.

    [3671] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3672] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3673] Assembly of the peptide fragment was in the following sequence:

    [3674] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3675] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3676] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3677] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3678] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 209 in Table 2.

    [3679] Example 210 is shown in Table 1.

    [3680] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3681] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1. Assembly of the peptide fragment was in the following sequence:

    [3682] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3683] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3684] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-.sup.DGlu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of .sup.DGlu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3685] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-Hiv.

    [3686] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 210 in Table 2.

    [3687] Example 211, 212 and 213 are shown in Table 1.

    [3688] Procedure D, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3689] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3690] Assembly of the peptide fragment was in the following sequence:

    [3691] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3692] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method E as described above.

    [3693] The peptides were synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.7, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.7 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3694] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-Hiv.

    [3695] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 211, 212 and 213 in Table 2.

    [3696] Example 214 is shown in Table 1.

    [3697] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3698] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3699] Assembly of the peptide fragment was in the following sequence:

    [3700] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3701] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3702] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-.sup.DGlu(Allyl)-OH for addition of the amino acid residue at P.sup.7, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of .sup.DGlu at P.sup.7 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3703] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-Hiv.

    [3704] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 214 in Table 2.

    [3705] Example 216 is shown in Table 1.

    [3706] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3707] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3708] Assembly of the peptide fragment was in the following sequence:

    [3709] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.1.

    [3710] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3711] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3712] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3713] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 216 in Table 2.

    [3714] Example 217 is shown in Table 1.

    [3715] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3716] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3717] Assembly of the peptide fragment was in the following sequence:

    [3718] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.1.

    [3719] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3720] The peptide was synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin), using Fmoc-.sup.DGlu(Allyl)-OH for addition of the amino acid residue at P.sup.6, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of .sup.DGlu at P.sup.6 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3721] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-Hiv.

    [3722] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 217 in Table 2.

    [3723] Example 218 is shown in Table 1.

    [3724] Procedure M1, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3725] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3726] Assembly of the peptide fragment was in the following sequence:

    [3727] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3728] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3729] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at P.sup.11 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3730] Resin-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3731] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 218 in Table 2.

    [3732] Example 228 is shown in Table 1.

    [3733] Procedure M1, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3734] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3735] Assembly of the peptide fragment was in the following sequence:

    [3736] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3737] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3738] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at C. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3739] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3740] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.1 and X.sup.12, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 228 in Table 2.

    [3741] Examples 229, and 230 are shown in Table 1.

    [3742] Procedure Q, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3743] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3744] Assembly of the peptide fragment was in the following sequence:

    [3745] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3746] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3747] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3748] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3749] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, and full deprotection were performed as indicated in procedure Q above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 229, and 230 in Table 2.

    [3750] Examples 232 and 233 are shown in Table 1.

    [3751] Procedure A, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3752] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3753] Assembly of the peptide fragment was in the following sequence:

    [3754] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1.

    [3755] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method B as described above.

    [3756] The peptides were synthesized starting with the amino alcohol Fmoc-Throl(tBu), which was grafted to the resin (Fmoc-Throl(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3757] Resin-Throl-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3758] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure A above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 232 and 233 in Table 2.

    [3759] Examples 234 and 235 are shown in Table 1.

    [3760] Procedure M1, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3761] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3762] Assembly of the peptide fragment was in the following sequence:

    [3763] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3764] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3765] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3766] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3767] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptides from the resin, formation of the disulfide interstrand linkages between P.sup.2 and P.sup.11 and between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 234 and 235 in Table 2.

    [3768] Example 236 is shown in Table 1.

    [3769] Procedure D, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3770] (I) The protected peptide fragment (module B and linker L) was synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3771] Assembly of the peptide fragment was in the following sequence:

    [3772] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3773] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method E as described above.

    [3774] The peptide was synthesized starting with the amino alcohol Fmoc-Glyol, which was grafted to the resin (Fmoc-Glyol-2-chlorotrityl resin), using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3775] Resin-Glyol-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-Hiv.

    [3776] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure D above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 236 in Table 2.

    [3777] Examples 237 to 240 are shown in Table 1.

    [3778] Procedure M1, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3779] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3780] Assembly of the peptide fragment was in the following sequence:

    [3781] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3782] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3783] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3784] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3785] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.4 and P.sup.9, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 237 to 240 in Table 2.

    [3786] Example 243 is shown in Table 1.

    [3787] Procedure M1, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3788] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3789] Assembly of the peptide fragment was in the following sequence:

    [3790] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3791] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3792] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.13 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3793] Resin-X.sup.13-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3794] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 243 in Table 2.

    [3795] Example 241 is shown in Table 1.

    [3796] Procedure E, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3797] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3798] Assembly of the peptide fragment was in the following sequence:

    [3799] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3800] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method F as described above.

    [3801] The peptide was synthesized starting with the amino acid Fmoc-.sup.DAla-OH, which was grafted to the resin (Fmoc-.sup.DAla-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3802] Resin-.sup.DAla-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3803] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure E above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 241 in Table 2.

    [3804] Example 242 is shown in Table 1.

    [3805] Procedure E, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3806] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3807] Assembly of the peptide fragment was in the following sequence:

    [3808] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3809] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method F as described above.

    [3810] The peptide was synthesized starting with the amino acid Fmoc-.sup.DSer(tBu)-OH, which was grafted to the resin (Fmoc-.sup.DSer(tBu)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3811] Resin-.sup.DSer-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3812] Subsequently, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure E above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 242 in Table 2.

    [3813] Example 244 is shown in Table 1.

    [3814] Procedure M1, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3815] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3816] Assembly of the peptide fragment was in the following sequence:

    [3817] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3818] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3819] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.13 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3820] Resin-X.sup.13-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3821] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between X.sup.13 and X.sup.14, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 244 in Table 2.

    [3822] Examples 245, 250, and 383 are shown in Table 1.

    [3823] Procedure P, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3824] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3825] Assembly of the peptide fragment was in the following sequence:

    [3826] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3827] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method L as described above.

    [3828] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.13 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5 and using 3-(tritylthio)propionic acid for addition of the thiol-substituted acyl residue at X.sup.14. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3829] Resin-X.sup.13-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3830] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between X.sup.13 and X.sup.14, and full deprotection were performed as indicated in procedure P above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 245, 250, and 383 in Table 2.

    [3831] Example 246 is shown in Table 1.

    [3832] Procedure M1, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3833] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3834] Assembly of the peptide fragment was in the following sequence:

    [3835] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3836] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3837] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.13 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3838] Resin-X.sup.13-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3839] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.9, and full deprotection were performed as indicated in procedure M1 above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 246 in Table 2.

    [3840] Example 247, 248 and 249 are shown in Table 1.

    [3841] Procedure Q, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3842] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3843] Assembly of the peptide fragment was in the following sequence:

    [3844] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3845] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3846] The peptide was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3847] Resin-X.sup.13-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3848] Subsequently, acylation with acetic acid at X.sup.14, cleavage of the peptides from the resin, and full deprotection were performed as indicated in procedure Q above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 247, 248 and 249 in Table 2.

    [3849] Examples 367 to 371, 373, 374, 375, 377, 378, and 380 are shown in Table 1. Procedure M2, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3850] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3851] Assembly of the peptide fragments was in the following sequence:

    [3852] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3853] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3854] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.13 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3855] Resin-X.sup.13-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3856] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, full deprotection, and formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11 were performed as indicated in procedure M2 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 367 to 371, 373, 374, 375, 377, 378, and 380 in Table 2.

    [3857] Example 372, 376, 379, 381, and 382 are shown in Table 1.

    [3858] Procedure O, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3859] (I) The protected peptide fragments (module B and linker L) were synthesized as indicated above in the corresponding section in the synthesis of Ex. 1.

    [3860] Assembly of the peptide fragments was in the following sequence:

    [3861] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3862] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method K as described above.

    [3863] The peptides were synthesized starting with an appropriately protected Fmoc amino acid which was used in the first coupling cycle for grafting the amino acid residue at X.sup.13 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3864] Resin-X.sup.13-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1-X.sup.14.

    [3865] Subsequently, cleavage of the peptides from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure O above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 372, 376, 379, 381, and 382 in Table 2.

    [3866] Examples 285, 286, 288 and 292 are shown in Table 1.

    [3867] Procedure R as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3868] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3869] Assembly of the peptide fragments was in the following sequence:

    [3870] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3871] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3872] The peptides were synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1.

    [3873] Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3874] Resin-Ser-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3875] Subsequently, acylation with acetic acid at P.sup.1, allyl deprotection at P.sup.2, ivDde deprotection at P.sup.11, and formation of the lactam interstrand linkage by an amide bond between the liberated side-chain functional groups of the amino acid residue at P.sup.2 and Dab at P.sup.11, cleavage of the peptides from the resin, and full deprotection were performed as indicated in procedure P above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 285, 286, 288 and 292 in Table 2.

    [3876] Examples 304 and 347 are shown in Table 1.

    [3877] Procedure S, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3878] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3879] Assembly of the peptide fragments was in the following sequence:

    [3880] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3881] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3882] The peptides were synthesized starting with the amino acid Fmoc-Ser(tBu)-OH, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5, using Fmoc-Asp(2-PhiPr)-OH for addition of the amino acid residue at P.sup.11, and using alpha-hydroxyisovaleric acid (Hiv) for addition of the hydroxy acid residue at P.sup.1. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3883] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3884] Subsequently, removal of the alloc protecting group at P.sup.2, cleavage of the peptides from the resin and removal of the 2-phenyl-isopropyl protecting group at P.sup.11, formation of the lactam interstrand linkage by an amide bond between the liberated side-chain functional groups of the residues at P.sup.2 and at P.sup.11, and full deprotection were performed as indicated in procedure Q above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 304 and 347, in Table 2.

    [3885] Examples 366 is shown in Table 1.

    [3886] Procedure M2, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3887] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3888] Assembly of the peptide fragment was in the following sequence:

    [3889] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3890] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method J as described above.

    [3891] The peptides was synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-.sup.DGlu(Allyl)-OH for addition of the amino acid residue at P.sup.7. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of .sup.DGlu at P.sup.7 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3892] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3893] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, full deprotection, and formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11 were performed as indicated in procedure M2 above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 366 in Table 2.

    [3894] Examples 354 to 365 are shown in Table 1.

    [3895] Procedure M2, as described above, was used for the preparation of the peptides, applying an on-resin fragment coupling strategy.

    [3896] (I) The protected peptide fragments (module B and linker L) were synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3897] Assembly of the peptide fragments was in the following sequence:

    [3898] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3899] (II) The fully protected peptides (module A, module B and linker L) were assembled on solid support according to method J as described above.

    [3900] The peptides were synthesized starting with an appropriately protected Fmoc-amino acid, which was used in the first coupling cycle for grafting the amino acid residue at X.sup.12 to Sieber amide resin, and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.7. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.7 and the α-amino group of Dab at L.sup.1. Assembly of the peptides was in the following sequence, showing only residues of module A:

    [3901] Resin-X.sup.12-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3902] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptides from the resin, full deprotection, and formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11 were performed as indicated in procedure M2 above. Finally, the peptides were purified, as described above, and characterized by HPLC-MS. For analytical data, see Ex. 354 to 365 in Table 2.

    [3903] Example 384 is shown in Table 1.

    [3904] Procedure F, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3905] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3906] Assembly of the peptide fragment was in the following sequence:

    [3907] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3908] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3909] The peptide was synthesized starting with the amino acid Fmoc-Cys(Trityl)-OH, which was grafted to the resin (Fmoc-Cys(Trityl)-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3910] Resin-Cys-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3911] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure F above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see 384 in Table 2.

    [3912] Example 385 is shown in Table 1.

    [3913] Procedure F, as described above, was used for the preparation of the peptide, applying an on-resin fragment coupling strategy.

    [3914] (I) The protected peptide fragment (module B and linker L) was synthesized as described above in the corresponding section in the synthesis of Ex. 1.

    [3915] Assembly of the peptide fragment was in the following sequence:

    [3916] Resin-Thr-Q.sup.6-Q.sup.5-Q.sup.4-Q.sup.3-Q.sup.2-Q.sup.1-L.sup.3-L.sup.2-L.sup.1.

    [3917] (II) The fully protected peptide (module A, module B and linker L) was assembled on solid support according to method G as described above.

    [3918] The peptide was synthesized starting with the amino acid Fmoc-Leu(3R)OtBu-OH, which was grafted to the resin (Fmoc-Leu(3R)OtBu-2-chlorotrityl resin) and using Fmoc-Glu(Allyl)-OH for addition of the amino acid residue at P.sup.5. Coupling of the protected peptide fragment (module B and linker L) was performed as indicated in the corresponding section of procedure A above by formation of an amide bond between the γ-carboxyl group of Glu at P.sup.5 and the α-amino group of Dab at L.sup.1. Assembly of the peptide was in the following sequence, showing only residues of module A:

    [3919] Resin-Leu(3R)OH-P.sup.11-P.sup.10-P.sup.9-P.sup.8-P.sup.7-P.sup.6-P.sup.5-P.sup.4-P.sup.3-P.sup.2-P.sup.1.

    [3920] Subsequently, acylation with acetic acid at P.sup.1, cleavage of the peptide from the resin, formation of the disulfide interstrand linkage between P.sup.2 and P.sup.11, and full deprotection were performed as indicated in procedure F above. Finally, the peptide was purified, as described above, and characterized by HPLC-MS. For analytical data, see 385 in Table 2.

    TABLE-US-00002 TABLE 1 Examples (Ex.) In the below-mentioned examples, amino acid residues are connected in either direction from the α carbonyl (C═O) point of attachment to the α nitrogen (N) of the next element, unless otherwise indicated. Other linkages, residues, connection of residues and modifications are as specified. Ex. No. Sequence Ex. 1 .sup.a) b) c) [00069]embedded image Ex 2 .sup.a) b) c) [00070]embedded image Ex 3 .sup.a) b) c) [00071]embedded image Ex 4 .sup.a) b) c) [00072]embedded image Ex 5 .sup.a) b) c) [00073]embedded image Ex 6 .sup.a) [00074]embedded image Ex 7 .sup.a) e) [00075]embedded image Ex 8 .sup.a) [00076]embedded image Ex 9 .sup.a) [00077]embedded image Ex 10 .sup.a) [00078]embedded image Ex 11 .sup.a) [00079]embedded image Ex 12 .sup.a) [00080]embedded image Ex 13 .sup.a) [00081]embedded image Ex 14 .sup.a) [00082]embedded image Ex 15 .sup.f) [00083]embedded image Ex 16 .sup.f) [00084]embedded image Ex 17 .sup.f) [00085]embedded image Ex 18 .sup.f) [00086]embedded image Ex 19 .sup.f) [00087]embedded image Ex 20 .sup.f) [00088]embedded image Ex 21 .sup.f) [00089]embedded image Ex 22 .sup.f) [00090]embedded image Ex 23 .sup.f) [00091]embedded image Ex 24 .sup.e) f) [00092]embedded image Ex 25 .sup.f) [00093]embedded image Ex 26 .sup.f) [00094]embedded image Ex 27 .sup.f) [00095]embedded image Ex 28 .sup.f) [00096]embedded image Ex 29 .sup.f) [00097]embedded image Ex 30 .sup.f) [00098]embedded image Ex 31 .sup.f) [00099]embedded image Ex 32 .sup.f) [00100]embedded image Ex 33 .sup.f) [00101]embedded image Ex 34 .sup.f) [00102]embedded image Ex 35 .sup.a) [00103]embedded image Ex 36 .sup.f) [00104]embedded image Ex 37 .sup.f) [00105]embedded image Ex 38 .sup.f) [00106]embedded image Ex 39 .sup.a) [00107]embedded image Ex 40 .sup.a) [00108]embedded image Ex 41 .sup.a) [00109]embedded image Ex 42 .sup.a) [00110]embedded image Ex 43 .sup.a) [00111]embedded image Ex 44 .sup.a) [00112]embedded image Ex 45 .sup.a) [00113]embedded image Ex 46 .sup.a) [00114]embedded image Ex 47 .sup.a) [00115]embedded image Ex 48 .sup.a) [00116]embedded image Ex 49 .sup.a) [00117]embedded image Ex 50 .sup.a) [00118]embedded image Ex 51 .sup.a) [00119]embedded image Ex 52 .sup.a) [00120]embedded image Ex 53 .sup.a) [00121]embedded image Ex 54 .sup.a) [00122]embedded image Ex 55 .sup.g) [00123]embedded image Ex 56 .sup.g) [00124]embedded image Ex 57 .sup.a) [00125]embedded image Ex 58 .sup.a) h) [00126]embedded image Ex 59 .sup.a) h) [00127]embedded image Ex 60 .sup.a) h) [00128]embedded image Ex 61 .sup.a) h) [00129]embedded image Ex 62 .sup.a) [00130]embedded image Ex 63 .sup.a) [00131]embedded image Ex 64 .sup.a) [00132]embedded image Ex 65 .sup.a) [00133]embedded image Ex 66 .sup.a) [00134]embedded image Ex 67 .sup.a) [00135]embedded image Ex 68 .sup.a) [00136]embedded image Ex 69 .sup.a) h) [00137]embedded image Ex 70 .sup.a) h) [00138]embedded image Ex 71 .sup.a) b) [00139]embedded image Ex 72 .sup.a) h) [00140]embedded image Ex 73 .sup.a) h) [00141]embedded image Ex 74 .sup.a) h) [00142]embedded image Ex 75 .sup.a) h) [00143]embedded image Ex 76 .sup.a) h) [00144]embedded image Ex 77 .sup.a) h) [00145]embedded image Ex 78 .sup.a) h) [00146]embedded image Ex 79 .sup.a) h) [00147]embedded image Ex 80 .sup.a) h) [00148]embedded image Ex 81 .sup.a) h) [00149]embedded image Ex 82 .sup.a) h) [00150]embedded image Ex 83 .sup.a) h) [00151]embedded image Ex 84 .sup.a) h) [00152]embedded image Ex 85 .sup.a) h) [00153]embedded image Ex 86 .sup.a) b) [00154]embedded image Ex 87 .sup.a) h) [00155]embedded image Ex 88 .sup.a) h) [00156]embedded image Ex 89 .sup.a) h) [00157]embedded image Ex 90 .sup.a) h) [00158]embedded image Ex 91 .sup.a) h) [00159]embedded image Ex 92 .sup.a) h) [00160]embedded image Ex 93 .sup.a) h) [00161]embedded image Ex 94 .sup.a) h) [00162]embedded image Ex 95 .sup.a) h) [00163]embedded image Ex 96 .sup.a) b) [00164]embedded image Ex 97 .sup.a) h) [00165]embedded image Ex 98 .sup.a) b) [00166]embedded image Ex 99 .sup.a) e) [00167]embedded image Ex 100 .sup.a) [00168]embedded image Ex 101 .sup.a) h) [00169]embedded image Ex 102 .sup.a) h) [00170]embedded image Ex 103 .sup.a) h) [00171]embedded image Ex 104 .sup.a) h) [00172]embedded image Ex 105 .sup.a) h) [00173]embedded image Ex 106 .sup.a) h) [00174]embedded image Ex 107 .sup.a) h) [00175]embedded image Ex 108 .sup.a) h) [00176]embedded image Ex 109 .sup.a) h) [00177]embedded image Ex 110 .sup.a) h) [00178]embedded image Ex 111 .sup.a) h) [00179]embedded image Ex 112 .sup.a) h) [00180]embedded image Ex 113 .sup.a) h) [00181]embedded image Ex 114 .sup.a) [00182]embedded image Ex 115 .sup.a) e) [00183]embedded image Ex 116 .sup.a) b) [00184]embedded image Ex 117 .sup.a) [00185]embedded image Ex 119 .sup.a) [00186]embedded image Ex 120 .sup.a) [00187]embedded image Ex 121 .sup.a) [00188]embedded image Ex 122 .sup.a) [00189]embedded image Ex 123 .sup.a) b) [00190]embedded image Ex 124 .sup.a) b) [00191]embedded image Ex 125 .sup.a) [00192]embedded image Ex 126 .sup.a) [00193]embedded image Ex 127 .sup.a) h) [00194]embedded image Ex 128 .sup.a) [00195]embedded image Ex 129 .sup.a) b) [00196]embedded image Ex 130 .sup.a) [00197]embedded image Ex 131 .sup.a) [00198]embedded image Ex 132 .sup.a) [00199]embedded image Ex 133 .sup.a) [00200]embedded image Ex 134 .sup.a) [00201]embedded image Ex 135 .sup.a) [00202]embedded image Ex 136 .sup.a) [00203]embedded image Ex 137 .sup.a) [00204]embedded image Ex 138 .sup.a) [00205]embedded image Ex 140 .sup.a) [00206]embedded image Ex 141 .sup.a) [00207]embedded image Ex 142 .sup.a) [00208]embedded image Ex 143 .sup.a) [00209]embedded image Ex 144 .sup.a) [00210]embedded image Ex 145 .sup.a) [00211]embedded image Ex 146 .sup.g) [00212]embedded image Ex 147 .sup.g) [00213]embedded image Ex 148 .sup.g) [00214]embedded image Ex 149 .sup.g) [00215]embedded image Ex 150 .sup.a) [00216]embedded image Ex 151 .sup.a) [00217]embedded image Ex 152 .sup.a) [00218]embedded image Ex 153 .sup.a) [00219]embedded image Ex 154 .sup.a) [00220]embedded image Ex 155 .sup.a) [00221]embedded image Ex 156 .sup.a) [00222]embedded image Ex 157 .sup.a) e) [00223]embedded image Ex 158 .sup.a) [00224]embedded image Ex 159 .sup.a) [00225]embedded image Ex 160 .sup.a) e) [00226]embedded image Ex 161 .sup.a) e) [00227]embedded image Ex 162 .sup.a) h) [00228]embedded image Ex 163 .sup.a) h) [00229]embedded image Ex 164 .sup.a) e) [00230]embedded image Ex 165 .sup.a) e) [00231]embedded image Ex 166 .sup.a) e) [00232]embedded image Ex 167 .sup.a) e) [00233]embedded image Ex 168 .sup.a) e) [00234]embedded image Ex 169 .sup.a) e) [00235]embedded image Ex 170 .sup.a) e) [00236]embedded image Ex 171 .sup.a) e) [00237]embedded image Ex 172 .sup.a) h) [00238]embedded image Ex 173 .sup.a) h) [00239]embedded image Ex 174 .sup.a) h) [00240]embedded image Ex 175 .sup.a) [00241]embedded image Ex 176 .sup.a) [00242]embedded image Ex 177 .sup.a) [00243]embedded image Ex 178 .sup.a) [00244]embedded image Ex 179 .sup.a) [00245]embedded image Ex 180 .sup.a) [00246]embedded image Ex 181 .sup.a) [00247]embedded image Ex 182 .sup.a) [00248]embedded image Ex 183 .sup.a) [00249]embedded image Ex 184 .sup.a) [00250]embedded image Ex 185 .sup.a) [00251]embedded image Ex 186 .sup.a) [00252]embedded image Ex 187 .sup.a) [00253]embedded image Ex 188 .sup.a) h) [00254]embedded image Ex 189 .sup.a) h) [00255]embedded image Ex 190 .sup.a) h) [00256]embedded image Ex 191 .sup.a) h) [00257]embedded image Ex 192 .sup.a) h) [00258]embedded image Ex 193 .sup.a) h) [00259]embedded image Ex 194 .sup.a) h) [00260]embedded image Ex 195 .sup.a) h) [00261]embedded image Ex 196 .sup.a) b) [00262]embedded image Ex 197 .sup.a) h) [00263]embedded image Ex 198 .sup.a) h) [00264]embedded image Ex 199 .sup.a) h) [00265]embedded image Ex 200 .sup.a) h) [00266]embedded image Ex 201 .sup.a) h) [00267]embedded image Ex 202 .sup.a) h) [00268]embedded image Ex 203 .sup.a) h) [00269]embedded image Ex 204 .sup.a) h) [00270]embedded image Ex 205 .sup.a) [00271]embedded image Ex 206 .sup.a) [00272]embedded image Ex 207 .sup.a) [00273]embedded image Ex 208 .sup.a) [00274]embedded image Ex 209 .sup.a) h) [00275]embedded image Ex 210 .sup.a) h) [00276]embedded image Ex 211 .sup.a) h) [00277]embedded image Ex 212 .sup.a) h) [00278]embedded image Ex 213 .sup.a) h) [00279]embedded image Ex 214 .sup.a) h) [00280]embedded image Ex 215 .sup.a) [00281]embedded image Ex 216 .sup.a) h) [00282]embedded image Ex 217 .sup.a) h) [00283]embedded image Ex 218 .sup.a) [00284]embedded image Ex 219 .sup.a) [00285]embedded image Ex 220 .sup.a) [00286]embedded image Ex 221 .sup.a) [00287]embedded image Ex 222 .sup.a) [00288]embedded image Ex 223 .sup.a) [00289]embedded image Ex 224 .sup.a) [00290]embedded image Ex 225 .sup.a) [00291]embedded image Ex 226 .sup.a) [00292]embedded image Ex 227 .sup.a) [00293]embedded image Ex 228 .sup.a) [00294]embedded image Ex 229 [00295]embedded image Ex 230 [00296]embedded image Ex 232 .sup.a) b) [00297]embedded image Ex 233 .sup.a) b) [00298]embedded image Ex 234 .sup.a) [00299]embedded image Ex 235 .sup.a) [00300]embedded image Ex 236 .sup.a) h) [00301]embedded image Ex 237 .sup.a) [00302]embedded image Ex 238 .sup.a) [00303]embedded image Ex 239 .sup.a) [00304]embedded image Ex 240 .sup.a) [00305]embedded image Ex 241 .sup.a) [00306]embedded image Ex 242 .sup.a) [00307]embedded image Ex 243 .sup.a) [00308]embedded image Ex 244 .sup.a) [00309]embedded image Ex 245 .sup.a) c) i) [00310]embedded image Ex 246 .sup.a) [00311]embedded image Ex 247 [00312]embedded image Ex 248 [00313]embedded image Ex 249 [00314]embedded image Ex 250 .sup.a) c) i) [00315]embedded image Ex 251 .sup.a) [00316]embedded image Ex 252 .sup.a) [00317]embedded image Ex 253 .sup.a) [00318]embedded image Ex 254 .sup.a) [00319]embedded image Ex 255 .sup.a) [00320]embedded image Ex 256 .sup.a) [00321]embedded image Ex 257 .sup.a) [00322]embedded image Ex 258 .sup.a) [00323]embedded image Ex 259 .sup.a) [00324]embedded image Ex 260 .sup.a) [00325]embedded image Ex 261 .sup.a) [00326]embedded image Ex 262 .sup.a) [00327]embedded image Ex 263 .sup.a) [00328]embedded image Ex 264 .sup.a) [00329]embedded image Ex 265 .sup.g) [00330]embedded image Ex 266 .sup.a) [00331]embedded image Ex 267 .sup.a) [00332]embedded image Ex 268 .sup.a) [00333]embedded image Ex 269 .sup.a) [00334]embedded image Ex 270 .sup.a) e) [00335]embedded image Ex 271 .sup.a) e) [00336]embedded image Ex 272 .sup.a) [00337]embedded image Ex 273 .sup.g) [00338]embedded image Ex 274 .sup.a) e) [00339]embedded image Ex 275 .sup.a) [00340]embedded image Ex 276 .sup.a) [00341]embedded image Ex 277 .sup.a) e) [00342]embedded image Ex 278 .sup.a) [00343]embedded image Ex 279 .sup.g) [00344]embedded image Ex 280 .sup.a) [00345]embedded image Ex 281 .sup.a) [00346]embedded image Ex 282 .sup.a) [00347]embedded image Ex 283 .sup.a) [00348]embedded image Ex 284 .sup.a) [00349]embedded image Ex 285 .sup.g) [00350]embedded image Ex 286 .sup.g) [00351]embedded image Ex 287 .sup.g) [00352]embedded image Ex 288 .sup.g) [00353]embedded image Ex 289 .sup.a) [00354]embedded image Ex 290 .sup.g) [00355]embedded image Ex 291 .sup.g) [00356]embedded image Ex 292 .sup.g) [00357]embedded image Ex 293 .sup.g) [00358]embedded image Ex 294 .sup.a) [00359]embedded image Ex 295 .sup.a) [00360]embedded image Ex 296 .sup.a) [00361]embedded image Ex 297 .sup.a) [00362]embedded image Ex 298 .sup.a) [00363]embedded image Ex 299 .sup.a) [00364]embedded image Ex 300 .sup.a) [00365]embedded image Ex 301 .sup.a) e) [00366]embedded image Ex 302 .sup.g) [00367]embedded image Ex 303 .sup.g) [00368]embedded image Ex 304 .sup.g) e) [00369]embedded image Ex 305 .sup.a) [00370]embedded image Ex 306 .sup.a) [00371]embedded image Ex 307 .sup.a) [00372]embedded image Ex 308 .sup.a) [00373]embedded image Ex 309 .sup.a) [00374]embedded image Ex 310 .sup.a) [00375]embedded image Ex 311 .sup.a) [00376]embedded image Ex 312 .sup.a) [00377]embedded image Ex 313 .sup.a) [00378]embedded image Ex 314 .sup.a) [00379]embedded image Ex 315 .sup.a) [00380]embedded image Ex 316 .sup.a) [00381]embedded image Ex 317 .sup.a) [00382]embedded image Ex 318 .sup.a) [00383]embedded image Ex 319 .sup.g) [00384]embedded image Ex 320 .sup.g) [00385]embedded image Ex 321 .sup.g) [00386]embedded image Ex 322 .sup.g) [00387]embedded image Ex 323 .sup.g) [00388]embedded image Ex 324 .sup.g) [00389]embedded image Ex 325 .sup.g) [00390]embedded image Ex 326 .sup.g) [00391]embedded image Ex 327 .sup.g) [00392]embedded image Ex 328 .sup.a) [00393]embedded image Ex 329 .sup.a) [00394]embedded image Ex 330 .sup.a) [00395]embedded image Ex 331 .sup.a) [00396]embedded image Ex 332 .sup.a) [00397]embedded image Ex 333 .sup.a) [00398]embedded image Ex 334 .sup.a) [00399]embedded image Ex 335 .sup.a) [00400]embedded image Ex 336 .sup.a) [00401]embedded image Ex 337 .sup.a) [00402]embedded image Ex 338 .sup.a) [00403]embedded image Ex 339 .sup.a) [00404]embedded image Ex 340 .sup.a) e) [00405]embedded image Ex 341 .sup.g) [00406]embedded image Ex 342 .sup.a) [00407]embedded image Ex 343 .sup.a) [00408]embedded image Ex 344 .sup.a) e) [00409]embedded image Ex 345 .sup.a) [00410]embedded image Ex 346 .sup.g) [00411]embedded image Ex 347 .sup.g) e) [00412]embedded image Ex 348 .sup.g) [00413]embedded image Ex 349 .sup.g) [00414]embedded image Ex 350 .sup.a) [00415]embedded image Ex 351 .sup.g) [00416]embedded image Ex 352 .sup.a) [00417]embedded image Ex 353 .sup.a) [00418]embedded image Ex 354 .sup.a) [00419]embedded image Ex 355 .sup.a) [00420]embedded image Ex 356 .sup.a) [00421]embedded image Ex 357 .sup.a) [00422]embedded image Ex 358 .sup.a) [00423]embedded image Ex 359 .sup.a) [00424]embedded image Ex 360 .sup.a) [00425]embedded image Ex 361 .sup.a) [00426]embedded image Ex 362 .sup.a) [00427]embedded image Ex 363 .sup.a) [00428]embedded image Ex 364 .sup.a) [00429]embedded image Ex 365 .sup.a) [00430]embedded image Ex 366 .sup.a) [00431]embedded image Ex 367 .sup.a) [00432]embedded image Ex 368 .sup.a) [00433]embedded image Ex 369 .sup.a) [00434]embedded image Ex 370 .sup.a) [00435]embedded image Ex 371 .sup.a) [00436]embedded image Ex 372 .sup.a) e) [00437]embedded image Ex 373 .sup.a) [00438]embedded image Ex 374 .sup.a) [00439]embedded image Ex 375 .sup.a) [00440]embedded image Ex 376 .sup.a) e) [00441]embedded image Ex 377 .sup.a) [00442]embedded image Ex 378 .sup.a) [00443]embedded image Ex 379 .sup.a) e) [00444]embedded image Ex 380 .sup.a) [00445]embedded image Ex 381 .sup.a) e) [00446]embedded image Ex 382 .sup.a) e) [00447]embedded image Ex 383 .sup.a) [00448]embedded image Ex 384 .sup.a) [00449]embedded image Ex 385 .sup.a) [00450]embedded image .sup.a) Disulfide interstrand linkage(s) between indicated amino acid residues in module A, involving disulfide bond(s) between a pair(s) of side-chain thiol groups as specified. .sup.b) 1,2-amino alcohol residue attached to the C-terminal amino acid residue of module A, involving an amide bond between the α-carboxyl group of the C-terminal amino acid residue and the amino group of the amino alcohol residue. .sup.c) Acid residue attached to the N-terminal amino acid residue of module A, involving an amide bond between the carboxyl group of the acid residue and the α-amino group of the N-terminal amino acid residue. .sup.e) α-hydroxy acid residue attached to the N-terminal amino acid residue of module A, involving an amide bond between the carboxyl group of the hydroxy acid residue and the a-amino group of the N-terminal amino acid residue. .sup.f) Lactam linkage between the two indicated amino acid residues in module A, involving an amide bond between the side-chain amino group of the residue at P2 and the α-carboxyl group of the residue at P11. .sup.g) Lactam interstrand linkage between the two indicated amino acid residues in module A, involving an amide bond between a side-chain amino group and a side-chain carboxyl group. .sup.h) 1,2-amino alcohol residue attached to the C-terminal amino acid residue of module A, involving an amide bond between the α-carboxyl group of the C-terminal amino acid residue and the amino group of the amino alcohol residue, and α-hydroxy acid residue attached to the N-terminal amino acid residue of module A, involving an amide bond between the carboxyl group of the hydroxy acid residue and the α-amino group of the N-terminal amino acid residue. .sup.i) Disulfide interstrand linkage between the indicated amino acid residue and the indicated acid residue in module A, involving a disulfide bond between a pair of side-chain thiol groups as specified.

    TABLE-US-00003 TABLE 2 Analytical data Ex. Meth. .sup.a) MS RT .sup.b) Pur. .sup.c)  1 A 776.7 .sup.g) 4.11 87  2 A 795.8 .sup.g) 3.98 83  3 B 791.3 .sup.g) 3.55 80  4 B 791.3 .sup.g) 3.69 90  5 A 589.9 .sup.h) 3.93 91  6 A 785.4 .sup.g) 3.81 92  7 A 771.8 .sup.g) 3.96 92  8 A 771.4 .sup.g) 3.95 90  9 A 766.4 .sup.g) 3.52 88 10 A 775.8 .sup.g) 3.89 91 11 A 780.9 .sup.g) 3.75 79 12 A 771.9 .sup.g) 3.45 92 13 A 775.7 .sup.g) 3.69 77 14 A 780.0 .sup.g) 3.62 85 15 B 783.3 .sup.g) 3.62 94  16 .sup.d) A 778.8 .sup.g) 4.12 95 17 B 779.2 .sup.g) 3.99 74 18 A 774.3 .sup.g) 4.37 82 19 A 778.5 .sup.g) 4.11 83 20 B 783.5 .sup.g) 3.75 76 21 A 783.5 .sup.g) 4.29 77 22 A 774.3 .sup.g) 4.22 75 23 A 769.5 .sup.g) 4.37 71 24 B 760.5 .sup.g) 3.80 70 25 A 773.9 .sup.g) 4.34 84 26 A 795.2 .sup.g) 4.51 83 27 A 773.9 .sup.g) 4.85 83 28 A 773.9 .sup.g) 3.92 77 29 B 778.7 .sup.g) 3.55 75 30 A 783.2 .sup.g) 3.96 80  31 .sup.d) E 774.3 .sup.g) 6.84 95 32 B 778.5 .sup.g) 3.90 73 33 A 778.8 .sup.g) 4.35 81 34 A 778.5 .sup.g) 4.31 82 35 B 769.2 .sup.g) 3.82 77 36 A 790.2 .sup.g) 4.34 80 37 A 768.9 .sup.g) 3.92 76 38 A 773.8 .sup.g) 4.09 80  39 .sup.d) A 814.7 .sup.g) 3.64 95 40 A 842.3 .sup.g) 4.76 92  41 .sup.d) B 809.7 .sup.g) 3.28 92  42 .sup.d) B 800.7 .sup.g) 3.21 95  43 .sup.d) B 600.5 .sup.h) 3.03 92 44 C 814.4 .sup.g) 2.83 93 45 C 809.7 .sup.g) 2.79 95 46 C 810.3 .sup.g) 2.94 93 47 C 600.7 .sup.h) 2.62 95 48 C 600.4 .sup.h) 2.55 94 49 C 819.0 .sup.g) 2.78 92 50 A 603.9 .sup.h) 3.34 90 51 C 607.4 .sup.h) 2.62 84 52 A 814.5 .sup.g) 3.86 81 53 C 600.9 .sup.h) 2.70 92 54 C 607.9 .sup.h) 2.70 91 55 A 798.4 .sup.g) 3.54 93 56 A 803.0 .sup.g) 3.40 83 57 A 776.0 .sup.g) 3.40 88  58 .sup.d) B 796.5 .sup.g) 3.59 95 59 A 777.0 .sup.g) 3.97 80 60 A 796.5 .sup.g) 3.88 84 61 A 812.4 .sup.g) 3.92 81 62 A 809.9 .sup.g) 3.74 88 63 A 809.8 .sup.g) 3.57 89 64 A 809.8 .sup.g) 3.57 84 65 A 607.5 .sup.h) 3.82 93 66 A 809.7 .sup.g) 3.53 92 67 A 809.7 .sup.g) 3.81 89 68 A 809.9 .sup.g) 3.72 71 69 A 819.4 .sup.g) 3.90 92 70 A 820.0 .sup.g) 3.85 85 71 A 829.2 .sup.g) 3.87 92 72 A 786.4 .sup.g) 3.93 80 73 A 781.9 .sup.g) 3.97 78 74 A 801.3 .sup.g) 3.86 80 75 A 819.8 .sup.g) 3.85 79 76 A 806.0 .sup.g) 3.86 90 77 A 804.9 .sup.g) 3.57 93 78 A 796.7 .sup.g) 3.79 87 79 A 796.5 .sup.g) 3.89 86 80 A 796.5 .sup.g) 3.84 82 81 A 805.8 .sup.g) 3.84 87 82 A 806.0 .sup.g) 3.83 84 83 A 801.0 .sup.g) 3.82 85 84 A 607.9 .sup.h) 3.98 78 85 B 810.4 .sup.g) 3.77 78 86 A 815.0 .sup.g) 3.87 92 87 A 593.4 .sup.h) 3.98 84 88 A 796.7 .sup.g) 3.98 87 89 A 796.4 .sup.g) 3.69 81 90 B 810.4 .sup.g) 3.59 81 91 A 810.4 .sup.g) 3.87 87  92 .sup.d) A 800.5 .sup.g) 4.05 95 93 B 801.3 .sup.g) 3.72 82 94 A 810.0 .sup.g) 3.96 91 95 A 796.4 .sup.g) 3.78 88  96 .sup.d) A 810.2 .sup.g) 3.67 95 97 A 791.8 .sup.g) 3.62 82 98 A 805.4 .sup.g) 3.57 88 99 A 796.3 .sup.g) 3.83 90 100   A 800.4 .sup.g) 3.68 93 101   A 801.0 .sup.g) 3.82 73 102   A 801.0 .sup.g) 3.79 88 103   A 787.0 .sup.g) 3.77 82 104   A 796.4 .sup.g) 3.88 84 105 .sup.d) A 815.2 .sup.g) 3.85 95 106 .sup.d) B 791.8 .sup.g) 3.57 95 107 .sup.d) B 791.8 .sup.g) 3.59 95 108 .sup.d) A 791.8 .sup.g) 3.90 95 109 .sup.d) A 782.4 .sup.g) 3.60 95 110 .sup.d) A 797.2 .sup.g) 3.79 95 111 .sup.d) A 791.5 .sup.g) 3.82 95 112 .sup.d) A 791.8 .sup.g) 3.91 95 113 .sup.d) A 814.4 .sup.g) 3.55 95 114 .sup.d) A 805.0 .sup.g) 3.76 95 115 .sup.d) A 786.7 .sup.g) 3.68 95 116 .sup.d) A 796.0 .sup.g) 3.71 95 117 .sup.d) A 800.7 .sup.g) 3.78 95 119   A 805.0 .sup.g) 3.91 87 120   A 804.7 .sup.g) 3.72 81 121   A 805.2 .sup.g) 3.97 81 122   A 814.7 .sup.g) 4.51 78 123   A 800.8 .sup.g) 3.92 87 124   A 800.7 .sup.g) 3.91 75 125   A 805.2 .sup.g) 3.69 82 126   A 809.0 .sup.g) 3.62 79 127   A 738.3 .sup.g) 4.25 85 128 .sup.d) A 805.2 .sup.g) 3.74 95 129 .sup.d) E 814.9 .sup.g) 6.50 95 130 .sup.d) E 1193.2 .sup.f)  6.01 95 131 .sup.d) E 819.3 .sup.g) 6.28 95 132 .sup.d) A 800.8 .sup.g) 3.90 95 133 .sup.d) A 805.2 .sup.g) 3.87 95 134 .sup.d) A 829.0 .sup.g) 3.71 95 135 .sup.d) A 823.8 .sup.g) 3.72 95 136 .sup.d) A 795.8 .sup.g) 3.41 95 137 .sup.d) B 790.8 .sup.g) 3.03 95 138 .sup.d) D 814.9 .sup.g) 3.55 94 139 .sup.d) A 805.5 .sup.g) 3.41 95 140 .sup.d) D 805.5 .sup.g) 3.25 95 141 .sup.d) A 805.2 .sup.g) 3.68 95 142 .sup.d) A 805.2 .sup.g) 3.75 95 143 .sup.d) A 800.3 .sup.g) 3.57 94 144 .sup.d) A 809.8 .sup.g) 3.89 95 145 .sup.d) A 809.8 .sup.g) 3.86 95 146   A 802.8 .sup.g) 3.70 89 147   A 1196.8 .sup.f)  3.56 84 148   A 798.2 .sup.g) 3.74 88 149   A 793.3 .sup.g) 3.63 82 150 .sup.d) A 814.4 .sup.g) 3.66 95 151 .sup.d) A 823.9 .sup.g) 3.64 95 152 .sup.d) A 819.3 .sup.g) 3.67 95 153 .sup.d) A 818.8 .sup.g) 3.63 95 154 .sup.d) A 819.2 .sup.g) 3.72 94 155   B 819.2 .sup.g) 3.38 80 156   A 823.9 .sup.g) 3.74 82 157   B 805.5 .sup.g) 3.40 76 158   A 828.5 .sup.g) 3.67 89 159   A 833.2 .sup.g) 3.75 90 160   A 604.4 .sup.h) 3.98 87 161   B 604.3 .sup.h) 3.64 90 162   A 597.5 .sup.h) 3.97 88 163   A 796.4 .sup.g) 3.88 82 164   A 747.3 .sup.g) 4.37 88 165   A 746.9 .sup.g) 4.24 91 166   A 604.0 .sup.h) 3.79 90 167   A 593.3 .sup.h) 3.88 91 168   A 589.8 .sup.h) 4.04 89 169   A 604.2 .sup.h) 3.86 85 170   A 593.2 .sup.h) 3.92 87 171   A 786.3 .sup.g) 4.01 83 172   A 597.3 .sup.h) 3.76 91 173   A 781.8 .sup.g) 3.86 82 174   A 776.9 .sup.g) 3.97 79 175   A 815.3 .sup.g) 3.82 89 176   C 601.3 .sup.h) 2.71 84 177   C 604.5 .sup.h) 2.74 82 178   C 809.4 .sup.g) 2.88 95 179   C 804.4 .sup.g) 2.82 95 180   A 795.0 .sup.g) 3.54 79 181   A 804.4 .sup.g) 3.51 82 182   C 795.4 .sup.g) 2.68 94 183   A 795.4 .sup.g) 3.49 76 184   C 593.2 .sup.h) 2.62 82 185   A 800.0 .sup.g) 3.59 76 186   C 795.7 .sup.g) 2.74 92 187   A 802.3 .sup.g) 3.74 85 188 .sup.d) B 796.3 .sup.g) 3.63 95 189   A 824.4 .sup.g) 3.64 89 190   A 611.5 .sup.h) 3.64 94 191 .sup.d) A 815.0 .sup.g) 3.76 95 192   B 614.9 .sup.h) 3.41 81 193   B 796.0 .sup.g) 3.68 75 194   A 805.4 .sup.g) 4.00 88 195   A 1208.8 .sup.f)  4.05 84 196   A 805.2 .sup.g) 3.81 82 197   B 782.0 .sup.g) 3.60 78 198   A 791.4 .sup.g) 3.98 90 199 .sup.d) B 791.3 .sup.g) 3.66 95 200 .sup.d) B 791.4 .sup.g) 3.65 95 201 .sup.d) A 781.2 .sup.g) 3.89 95 202 .sup.d) B 790.8 .sup.g) 3.90 95 203 .sup.d) A 795.8 .sup.g) 3.95 95 204 .sup.d) A 811.2 .sup.g) 3.96 94 205   A 799.4 .sup.g) 3.58 82 206   A 813.7 .sup.g) 4.00 80 207   A 804.2 .sup.g) 4.03 81 208   A 808.4 .sup.g) 4.29 91 209   A 796.0 .sup.g) 4.13 74 210   A 796.4 .sup.g) 4.07 80 211   B 597.0 .sup.h) 3.64 76 212   A 781.7 .sup.g) 4.03 82 213   B 582.8 .sup.h) 3.75 74 214   A 582.9 .sup.h) 4.02 71 215 .sup.d) A 804.8 .sup.g) 3.76 95 216   A 737.7 .sup.g) 4.54 83 217   A 737.5 .sup.g) 4.40 83 218   A 610.7 .sup.h) 3.51 74 219 .sup.d) E 800.3 .sup.g) 6.60 95 220 .sup.d) E 1206.7 .sup.f)  6.75 95 221 .sup.d) A 824.2 .sup.g) 3.91 95 222 .sup.d) A 819.4 .sup.g) 3.76 95 223 .sup.d) A 824.8 .sup.g) 3.95 95 224 .sup.d) A 819.8 .sup.g) 3.49 95 225 .sup.d) A 843.0 .sup.g) 3.64 95 226 .sup.d) A 824.8 .sup.g) 3.78 95 227 .sup.d) E 814.5 .sup.g) 6.52 95 228   A 828.2 .sup.g) 3.97 92 229   A 808.8 .sup.g) 3.57 73 230   A 813.0 .sup.g) 3.73 76 232   A 828.4 .sup.g) 3.82 90 233   A 621.5 .sup.h) 3.87 81 234   A 857.1 .sup.g) 4.31 83 235   A 853.7 .sup.g) 4.09 82 236   A 810.4 .sup.g) 4.05 88 237   A 833.4 .sup.g) 3.62 78 238   A 837.4 .sup.g) 3.94 82 239   A 846.4 .sup.g) 4.01 73 240   A 851.8 .sup.g) 3.84 80 241   A 640.4 .sup.h) 3.59 72 242   C 644.3 .sup.h) 2.65 90 243 .sup.d) A 881.6 .sup.g) 3.62 95 244   A 857.8 .sup.g) 3.91 83 245   A 839.0 .sup.g) 4.04 74 246   A 875.4 .sup.g) 3.78 88 247   A 870.6 .sup.g) 3.45 73 248   A 870.6 .sup.g) 3.46 74 249   A 875.4 .sup.g) 3.81 92 250 .sup.d) A 862.2 .sup.g) 4.16 95 251 .sup.d) A 800.2 .sup.g) 3.78 95 252 .sup.d) B 809.8 .sup.g) 3.60 95 253 .sup.d) A 805.0 .sup.g) 3.93 95 254 .sup.d) A 795.5 .sup.g) 3.58 95 255 .sup.d) B 800.2 .sup.g) 3.36 95 256 .sup.d) A 800.4 .sup.g) 3.65 95 257 .sup.d) A 795.7 .sup.g) 3.66 95 258 .sup.d) B 800.2 .sup.g) 3.42 95 259 .sup.d) B 805.0 .sup.g) 3.64 95 260 .sup.d) A 791.4 .sup.g) 3.66 95 261 .sup.d) A 801.0 .sup.g) 3.48 95 262 .sup.d) A 805.4 .sup.g) 3.49 95 263 .sup.d) A 810.4 .sup.g) 3.58 95 264 .sup.e) A 800.2 .sup.g) 3.82 94 265 .sup.e) B 802.8 .sup.g) 3.49 90 266 .sup.d) B 814.5 .sup.g) 3.17 95 267 .sup.e) A 804.9 .sup.g) 3.84 97 268 .sup.e) A 814.3 .sup.g) 3.75 97 269 .sup.e) B 795.5 .sup.g) 3.44 96 270 .sup.e) A 786.4 .sup.g) 3.72 97 271 .sup.e) B 791.3 .sup.g) 3.48 98 272 .sup.e) A 805 .sup.g)   3.76 96 273 .sup.e) A 797.9 .sup.g) 3.70 98 274 .sup.e) A 772.5 .sup.g) 3.35 96 275 .sup.e) H 790.3 .sup.g) 6.69 96 276 .sup.e) B 795.7 .sup.g) 3.54 97 277 .sup.e) B 782.2 .sup.g) 3.52 95 278 .sup.e) A 800.4 .sup.g) 3.79 96 279 .sup.e) B 793.5 .sup.g) 3.40 92 280 .sup.e) I 800.5 .sup.g) 6.08 92 281 .sup.e) H 790.7 .sup.g) 6.57 96 282 .sup.e) A 800.5 .sup.g) 3.78 89 283 .sup.e) A 791.9 .sup.g) 3.36 93 284 .sup.e) A 796.7 .sup.g) 3.39 86 285 .sup.e) G 793.7 .sup.g) 3.38 98 286 .sup.e) A 798.3 .sup.g) 3.49 96 287 .sup.e) G 798.3 .sup.g) 3.25 98 288 .sup.e) G 798.3 .sup.g) 3.36 99 289 .sup.e) G 785.8 .sup.g) 3.51 98 290 .sup.e) G 783.7 .sup.g) 3.38 96 291 .sup.e) G 788.3 .sup.g) 3.36 99 292 .sup.e) G 783.5 .sup.g) 3.40 99 293 .sup.e) G 788.3 .sup.g) 3.29 98 294 .sup.d) A 795.5 .sup.g) 3.41 97 295 .sup.e) I 597.2 .sup.g) 6.08 97 296 .sup.e) H 800.5 .sup.g) 6.29 96 297 .sup.e) I 800.5 .sup.g) 5.91 97 298 .sup.d) A 785.5 .sup.g) 3.48 98 299 .sup.e) H 785.7 .sup.g) 6.61 96 300 .sup.e) A 795.3 .sup.g) 3.24 96 301 .sup.e) G 796 .sup.g)   3.40 97 302 .sup.e) G 802.9 .sup.g) 3.24 95 303 .sup.e) A 807.5 .sup.g) 3.66 99 304 .sup.e) G 789 .sup.g)   3.17 93 305 .sup.e) A 800.3 .sup.g) 3.87 96 306 .sup.e) A 805.3 .sup.g) 3.62 95 307 .sup.e) A 785.7 .sup.g) 3.66 95 308 .sup.e) G 800.7 .sup.g) 3.26 95 309 .sup.e) G 805.3 .sup.g) 3.31 98 310 .sup.e) A 800.5 .sup.g) 3.68 97 311 .sup.e) G 805 .sup.g)   3.30 95 312   G 795.5 .sup.g) 3.07 90 313   G 795.7 .sup.g) 3.13 90 314   A 804.9 .sup.g) 3.84 98 315 .sup.e) A 805 .sup.g)   3.76 95 316 .sup.d) A 805 .sup.g)   3.84 97 317 .sup.e) A 800.4 .sup.g) 3.67 94 318 .sup.e) A 795.9 .sup.g) 3.65 93 319 .sup.e) A 802.8 .sup.g) 3.62 95 320 .sup.e) G 798.3 .sup.g) 3.15 95 321 .sup.e) A 807.5 .sup.g) 3.41 94 322 .sup.e) A 802.8 .sup.g) 3.59 95 323 .sup.e) A 802.9 .sup.g) 3.67 97 324 .sup.e) A 807.3 .sup.g) 3.54 96 325 .sup.e) G 802.9 .sup.g) 3.32 95 326 .sup.e) A 807.4 .sup.g) 3.59 96 327 .sup.e) A 807.5 .sup.g) 3.59 97 328 .sup.e) A 812.8 .sup.g) 3.65 95 329 .sup.e) A 816.8 .sup.g) 3.53 95 330   A 809.3 .sup.g) 3.74 98 331 .sup.e) H 796.7 .sup.g) 5.64 96 332 .sup.e) I 795.9 .sup.g) 5.43 94 333 .sup.e) H 801.3 .sup.g) 5.60 92 334 .sup.e) H 805.3 .sup.g) 6.32 96 335 .sup.e) H 790.5 .sup.g) 6.60 97 336 .sup.e) I 809.5 .sup.g) 5.80 95 337 .sup.e) I 786.4 .sup.g) 6.36 96 338 .sup.e) H 795.9 .sup.g) 6.06 95 339 .sup.e) H 786.5 .sup.g) 5.68 97 340 .sup.e) G 795.9 .sup.g) 3.38 99 341 .sup.e) G 797.9 .sup.g) 3.16 99 342 .sup.e) A 800.5 .sup.g) 3.57 97 343 .sup.e) A 800.8 .sup.g) 3.21 92 344 .sup.e) A 786.5 .sup.g) 3.69 98 345 .sup.e) I 790.7 .sup.g) 6.30 96 346 .sup.e) G 783.3 .sup.g) 3.24 95 347 .sup.e) G 774.4 .sup.g) 3.14 95 348 .sup.e) A 792.9 .sup.g) 3.76 95 349 .sup.e) G 792.9 .sup.g) 2.75 96 350 .sup.e) H 790.7 .sup.g) 6.53 96 351 .sup.e) G 788 .sup.g)   3.25 97 352   A 823.2 .sup.g) 3.77 97 353   A 813.7 .sup.g) 3.72 96 354 .sup.e) G 804.9 .sup.g) 3.34 98 355 .sup.e) G 809.7 .sup.g) 3.36 96 356 .sup.e) A 800.5 .sup.g) 3.74 96 357 .sup.e) G 785.9 .sup.g) 3.59 97 358 .sup.e) G 812.9 .sup.g) 3.37 96 359 .sup.e) I 809.5 .sup.g) 5.94 97 360 .sup.e) G 790.5 .sup.g) 3.41 97 361 .sup.e) A 794.9 .sup.g) 3.91 96 362 .sup.e) G 804.5 .sup.g) 3.79 96 363 .sup.e) A 799.7 .sup.g) 4.01 96 364 .sup.e) G 805 .sup.g)   3.42 96 365 .sup.e) G 816.9 .sup.g) 3.30 98 366 .sup.e) G 804.9 .sup.g) 3.30 98 367 .sup.e) B 823.9 .sup.g) 3.39 98 368 .sup.e) A 828.8 .sup.g) 3.79 97 369 .sup.e) A 819.3 .sup.g) 3.58 96 370 .sup.e) F 824 .sup.g)   3.17 94 371 .sup.e) B 838.9 .sup.g) 3.46 96 372 .sup.e) B 829.5 .sup.g) 3.39 94 373 .sup.e) B 838.4 .sup.g) 3.40 97 374 .sup.e) A 838.9 .sup.g) 3.61 91 375 .sup.e) A 829.3 .sup.g) 3.59 97 376 .sup.e) A 801.2 .sup.g) 3.52 93 377 .sup.e) A 819.5 .sup.g) 3.65 98 378 .sup.e) A 823.9 .sup.g) 3.66 95 379 .sup.e) A 810.3 .sup.g) 3.69 94 380 .sup.e) A 824.9 .sup.g) 3.45 94 381 .sup.e) A 806.5 .sup.g) 3.33 95 382 .sup.e) A 795.9 .sup.g) 3.65 95 383 .sup.e) H 643.4 .sup.g) 6.95 92 384 .sup.e) G 771.5 .sup.g) 3.45 97 385 .sup.e) A 824.5 .sup.g) 3.91 95 .sup.a) Analytical method .sup.b) Retention time in [min] .sup.c) Purity in [%] .sup.d) Acetate salt .sup.e) Chloride salt .sup.f) MS: m/z for [M + 2H].sup.2+ .sup.g) MS: m/z for [M + 3H].sup.3+ .sup.h) MS: m/z for [M + 4H].sup.4+

    [3921] 2. Biological Methods

    [3922] 2.1 Preparation of the Peptides

    [3923] Lyophilized peptides were weighed on a Microbalance (Mettler MT5) and dissolved in sterile water to a final concentration of 1 mg/mL. Stock solutions were kept at +4° C., light protected.

    [3924] 2.2 Antimicrobial Activity of the Peptides

    [3925] The in vitro antimicrobial activities of the peptides were determined in 96-well plates (Greiner, polystyrene) by the standard CLSI broth microdilution method (Clinical and Laboratory Standards Institute 2014. Performance standards for antimicrobial susceptibility testing, 24th informational supplement. Approved standard CLSI M100-S24; Clinical and Laboratory Standards Institute, Wayne, Pa.). The following microorganisms were used to determine antibiotic activity of the peptides: Escherichia coli ATCC 25922, Klebsiella pneumoniae SSI #3010.sup.a), Acinetobacter baumannii DSM 30008, Pseudomonas aeruginosa ATCC 27853 and the clinical isolates Escherichia coli 926415.sup.b), Klebsiella pneumoniae 968733.sup.b), Acinetobacter baumannii 872842.sup.b), Enterobacter cloacae 848840.sup.b) and Escherichia coli MCR-1 Af45.sup.c). Before preparation of inocula, Escherichia coli MCR-1 Af45 was subcultured on Mueller-Hinton II (MH-cation adjusted) agar containing 2 μg/mL colistin. .sup.a) Obtained from Statens Serum Institut (SSI), Copenhagen, Denmark.sup.b) Obtained from International Health Management Associates, Inc. (IHMA Europe Sari), Epalinges, Switzerland.sup.c) Obtained from Prof. Patrice Nordmann, University of Fribourg, Fribourg, Switzerland

    [3926] Inocula of the microorganisms were diluted into Mueller-Hinton II (MH-cation adjusted) broth and compared with a 0.5 McFarland standard to give appr. 10.sup.6 colony forming units (CFU)/mL. Aliquots (90 μL) of inoculum were added to 10 μL of MH-II broth +P-80 (Polysorbate 80, 0.002% final concentration, v/v) containing the peptide in serial two-fold dilutions. Antimicrobial activities of the peptides were expressed as the minimal inhibitory concentration (MIC) in μg/mL at which no visible growth was observed after 18-20 hours of incubation at 35° C.

    [3927] 2.3 Hemolysis

    [3928] The peptides were tested for their hemolytic activity against human red blood cells (hRBC). Fresh hRBC were washed four times with phosphate buffered saline (PBS) and centrifuged for 10 min at 3000×g. Compounds (200 μg/mL) were incubated with 20% hRBC (v/v) for 1 h at 37° C. and shaking at 300 rpm. A value of 0% and 100% cell lysis, respectively, was determined by incubation of hRBC in the presence of PBS containing 10% water and 2% Triton X-100 in H.sub.2O, respectively. The samples were centrifuged, the supernatants were ˜7.5-fold diluted in PBS buffer and the optical densities (OD) were measured at 540 nm and blank corrected. The 100% lysis value (OD.sub.540Triton X-100) gave an OD.sub.540 of approximately 0.5-1.0.

    [3929] Percent hemolysis was calculated as follows: (OD.sub.540peptide/OD.sub.540Triton X-100)×100%.

    [3930] 2.4 Tolerability in a Mouse Model

    [3931] The tolerability of the peptides was tested in a mouse model at Pharmacology Discovery Services Taiwan Ltd, Taipei, Taiwan. The peptides were administered subcutaneously (s.c.) at 30 mg/kg or 40 mg/kg, respectively; twice at a 12-hr interval, for assessment of possible adverse effects in the Maximum Tolerated Dose (MTD) assay in male ICR (Institute of Cancer Research) mice. The peptides were dissolved in 0.9% NaCl at the concentrations either of 6 or 8 mg/mL, respectively, based on the free base molecular weight. The pH values of dosing solutions were adjusted to 6.5-7.6 before s.c. administration. A dosing volume at 5 mL/kg and a concentration of 6 or 8 mg/mL, respectively, was applied. The fresh prepared stock solution were stored at 4° C. during the study. Male ICR mice weighing 23±3 g were provided by BioLasco Taiwan (under Charles River Laboratories Licensee). Animals were acclimated for 3 days prior to use and were confirmed to be in good health. The peptides were administered s.c. at 30 mg/kg or 40 mg/kg, respectively, twice at a 12-hr interval, to groups of 3 ICR male mice and observed for the presence of acute toxic symptoms (mortality, convulsions, tremors, muscle relaxation, sedation, etc.) and autonomic effects (diarrhea, salivation, lacrimation, vasodilation, piloerection, etc.) during the first 30 min. The peptides were administered again at a 12-hr (two total doses) interval, following the first dose. The animals were then observed again for the presence of acute toxic symptoms and autonomic effects during the first 30 min. Mortality was observed at 0.5 and 12 hr following the first dose and again at 0.5, 1, 3, 24, 48, and 72 hr after the second dose of test articles.

    [3932] 2.5 Nephrotoxicity in a Mouse Model

    [3933] The nephrotoxicity of the peptides was tested in a mouse model at Fidelta Ltd, Zagreb, Croatia. Colistin B (polymyxin E2, acetate salt, individually synthesized, 95% purity) was provided by Polyphor Ltd (Allschwil, Switzerland). The purpose of the study was to evaluate the toxic potential of the peptides in male CD1 mice after 1 day of subcutaneous dosing (72 mg/kg/day), divided into 6 administrations (12 mg/kg). Stock solutions of the peptides were prepared in saline (7.2 mg/ml), pH adjusted if required to pH 6.5-7.6 before s.c. administration. The peptides were administered to the animals subcutaneously 6 times a day (every 2 hours). The study involved 7 groups of 5 males in control and dose groups. After 24 h from start of the first dosing the animals were euthanized (isoflurane anesthesia-Abbott, Netherlands and exsanguination). All animals were subjected to gross necropsy as rapidly as possible and their main tissues examined macroscopically. The kidneys were fixed in an appropriate fixative and preserved in 10% buffered formaldehyde for histopathological examination. After dehydration and embedding in paraffin wax, sections of the tissues were cut at 5 micrometer thickness and stained with haematoxylin and eosin.

    [3934] Semi-quantitative scoring of the kidneys was performed according to the following method:

    [3935] Lesions were rated as follows: mild acute tubular damage with tubular dilation, prominent nuclei and a few pale tubular casts (Grade 1); severe acute tubular damage with necrosis of tubular epithelial cells and numerous tubular casts (Grade 2); necrosis/infarction of tubules and glomeruli with or without papillary necrosis (Grade 3). The grades were given the following scores: grade 1=1, grade 2=4 and grade 3=10. Moreover, the percentages of kidney slides affected were scored as follows:

    [3936] <1%=0; 1 to 5%=1; 5 to <10%=2; 10 to <20%=3; 20 to <30%=4; 30 to <40%=5; and >40%=6.

    [3937] Subsequently, the overall kidney histology score was calculated as the product of percentage score and grade score. These scores were then expressed as a semi-quantitative score (SQS) on a scale of 0 to +5 for renal histological changes. These scores were assigned as follows: [3938] SQS 0=no significant change (overall score, <1) [3939] SQS +1=mild damage (overall score, 1 to <15) [3940] SQS +2=mild to moderate damage (overall score, 15 to <30) [3941] SQS +3=moderate damage (overall score, 30 to <45) [3942] SQS +4=moderate to severe damage (overall score, 45 to <60) [3943] SQS +5=severe damage (overall score, >60)

    [3944] (Yousef, J., Chen, G., Hill, P., Nation, R., Li, J., Antimicrobial Agents And Chemotherapy [P], 2011, Vol 55, issue 9, American Society for Microbiology, USA, pp. 4044-4049).

    [3945] The results of the experiments described in 2.2-2.5 are indicated in Tables 3, 4, 5, 6 and 7 herein below.

    TABLE-US-00004 TABLE 3 Minimal inhibitory concentrations (MIC) in Mueller-Hinton II broth and Hemolysis Escherichia Klebsiella Acinetobacter Pseudomonas coli pneumoniae baumannii aeruginosa ATCC SSI DSM ATCC Hemolysis 25922 #3010 30008 27853 at 200 MIC MIC MIC MIC μg/mL Ex. [μg/mL] [μg/mL] [μg/mL] [μg/mL] [%] 1 0.125 0.5 0.125 0.125 <1 2 0.125 0.5 0.125 0.25 <1 3 0.125 0.125 0.0625 0.125 <1 4 0.125 0.125 0.0625 0.125 1 5 0.0625 0.125 0.0625 0.125 <1 6 0.125 0.25 0.125 0.125 2 7 0.125 0.125 0.0625 0.125 <1 8 0.0625 0.125 0.125 0.125 <1 9 0.125 0.125 0.125 0.125 <1 10 0.25 0.25 0.125 0.125 <1 11 0.125 0.125 0.125 0.25 1 12 0.0625 0.25 0.125 0.125 2 13 0.125 0.125 0.125 0.125 <1 14 0.25 0.5 0.5 0.25 <1 15 0.0625 0.125 0.125 0.25 <1 16 0.0625 0.0625 0.0625 0.25 <1 17 0.0625 0.125 0.0625 0.25 <1 18 0.0625 0.125 0.0625 0.25 1 19 0.125 0.125 0.125 0.25 <1 20 0.125 0.125 0.125 0.25 <1 21 0.25 0.5 0.5 0.5 <1 22 0.0625 0.125 0.0625 0.5 <1 23 0.0625 0.125 0.0625 0.25 <1 24 0.125 0.125 0.125 0.25 <1 25 0.0625 0.125 0.0625 0.25 <1 26 0.0625 0.125 0.03125 0.25 1 27 0.0625 0.25 0.0625 0.5 <1 28 0.125 0.125 0.125 0.25 <1 29 0.0625 0.125 0.125 0.25 1 30 0.0625 0.125 0.125 0.25 <1 31 0.03125 0.0625 0.03125 0.25 <1 32 0.0625 0.125 0.0625 0.25 <1 33 0.0625 0.125 0.0625 0.25 <1 34 0.0625 0.125 0.03125 0.25 <1 35 0.125 0.25 0.125 0.25 <1 36 0.0625 0.125 0.0625 0.25 <1 37 0.25 0.25 0.125 0.5 1 38 0.0625 0.125 0.125 0.25 n.d. 39 0.0625 0.0625 0.0625 0.125 <1 40 0.125 0.5 1 0.25 2 41 0.0625 0.125 0.0625 0.25 <1 42 0.125 0.25 0.5 0.25 <1 43 0.25 0.25 0.5 0.5 <1 44 0.0625 0.125 0.125 0.125 <1 45 0.0625 0.125 0.0625 0.125 <1 46 0.0625 0.125 0.0625 0.125 2 47 0.0625 0.125 0.125 0.125 <1 48 0.25 0.25 0.25 0.125 <1 49 0.125 0.125 0.0625 0.125 <1 50 0.125 0.125 0.25 0.25 <1 51 0.25 0.125 0.5 0.125 <1 52 0.25 0.25 1 0.25 <1 53 0.125 0.125 0.25 0.125 <1 54 0.0625 0.25 0.25 0.25 <1 55 0.25 0.5 0.5 0.25 2 56 0.5 1 1 0.5 <1 57 0.125 0.25 0.125 0.25 3 58 0.0625 0.125 0.0625 0.25 1 59 0.125 0.125 0.125 0.125 <1 60 0.0625 0.125 0.0625 0.125 <1 61 0.125 0.0625 0.0625 0.125 3 62 0.125 0.0625 0.0625 0.125 <1 63 0.125 0.125 0.125 0.125 <1 64 0.125 0.125 0.0625 0.125 <1 65 0.125 0.25 0.125 0.125 <1 66 0.0625 0.125 0.25 0.25 <1 67 0.125 0.5 0.25 0.25 <1 68 0.25 0.125 0.25 0.5 <1 69 0.0625 0.0625 0.0625 0.125 2 70 0.125 0.125 0.0625 0.125 <1 71 0.0625 0.125 0.0625 0.125 1 72 0.0625 0.125 0.0625 0.125 <1 73 0.0625 0.125 0.0625 0.25 <1 74 0.0625 0.0625 0.0625 0.25 <1 75 0.0625 0.125 0.0625 0.125 <1 76 0.0625 0.125 0.0625 0.25 1 77 0.125 0.125 0.125 0.125 <1 78 0.03125 0.25 0.0625 0.125 <1 79 0.0625 0.0625 0.03125 0.125 <1 80 0.03125 0.125 0.125 0.125 <1 81 0.0625 0.0625 0.125 0.125 <1 82 0.0625 0.0625 0.125 0.25 <1 83 0.0625 0.0625 0.0625 0.125 <1 84 0.0625 0.125 0.125 0.25 <1 85 0.0625 0.125 0.25 0.25 1 86 0.125 0.125 0.0625 0.125 <1 87 0.0625 0.125 0.0625 0.125 <1 88 0.0625 0.125 0.03125 0.125 <1 89 0.125 0.125 0.0625 0.25 <1 90 0.0625 0.125 0.125 0.25 <1 91 0.0625 0.25 0.125 0.25 <1 92 0.0625 0.0625 0.125 0.125 <1 93 0.125 0.125 0.25 0.25 <1 94 0.0625 0.0625 0.125 0.25 <1 95 0.03125 0.125 0.0625 0.125 <1 96 0.0625 0.125 0.125 0.125 <1 97 0.25 0.125 0.25 0.25 <1 98 0.125 0.25 0.25 0.25 <1 99 0.0625 0.125 0.0625 0.125 1 100 0.03125 0.125 0.0625 0.125 <1 101 0.0625 0.125 0.0625 0.125 <1 102 0.0625 0.25 0.0625 0.25 <1 103 0.0625 0.125 0.0625 0.125 1 104 0.0625 0.125 0.125 0.25 1 105 0.0625 0.0625 0.03125 0.125 <1 106 0.0625 0.125 0.0625 0.125 <1 107 0.0625 0.125 0.0625 0.125 <1 108 0.0625 0.0625 0.03125 0.125 2 109 0.03125 0.0625 0.03125 0.125 <1 110 0.0625 0.0625 0.0625 0.125 2 111 0.125 0.125 0.03125 0.25 <1 112 0.0625 0.0625 0.0625 0.125 <1 113 0.0625 0.0625 0.125 0.125 <1 114 0.03125 0.0625 0.0625 0.125 <1 115 0.0625 0.0625 0.0625 0.125 <1 116 0.03125 0.03125 0.03125 0.125 <1 117 0.0625 0.0625 0.015625 0.125 2 119 0.0625 0.0625 0.0625 0.125 <1 120 0.125 0.0625 0.0625 0.125 1 121 0.0625 0.125 0.0625 0.125 <1 122 0.25 0.5 0.25 0.5 1 123 0.015625 0.0625 0.015625 0.0625 <1 124 0.0625 0.125 0.0625 0.125 2 125 0.0625 0.0625 0.125 0.125 2 126 0.125 0.125 0.125 0.25 <1 127 0.0625 0.25 0.0625 0.5 2 128 0.03125 0.0625 0.03125 0.125 <1 129 0.03125 0.0625 0.0625 0.25 <1 130 0.03125 0.0625 0.015625 0.125 1 131 0.0625 0.125 0.25 0.25 <1 132 0.03125 0.125 0.03125 0.125 2 133 0.03125 0.125 0.0625 0.25 2 134 0.03125 0.03125 0.03125 0.125 3 135 0.03125 0.0625 0.03125 0.125 <1 136 0.03125 0.0625 0.03125 0.25 3 137 0.03125 0.0625 0.0625 0.125 1 138 0.03125 0.03125 0.03125 0.125 <1 139 0.0625 0.0625 0.0625 0.25 2 140 0.125 0.125 0.125 0.25 <1 141 0.03125 0.03125 0.03125 0.125 2 142 0.0625 0.03125 0.03125 0.125 <1 143 0.03125 0.0625 0.0625 0.125 2 144 0.03125 0.0625 0.0625 0.125 <1 145 0.0625 0.125 0.0625 0.125 2 146 0.0625 0.0625 0.0625 0.125 <1 147 0.0625 0.0625 0.0625 0.125 <1 148 0.03125 0.0625 0.03125 0.125 <1 149 0.0625 0.125 0.0625 0.125 <1 150 0.03125 0.125 0.0625 0.125 <1 151 0.03125 0.0625 0.0625 0.125 <1 152 0.125 0.25 0.125 0.25 <1 153 0.0625 0.0625 0.03125 0.125 <1 154 0.03125 0.0625 0.015625 0.125 <1 155 0.0625 0.125 0.0625 0.125 1 156 0.03125 0.125 0.0625 0.125 <1 157 0.0625 0.125 0.125 0.25 <1 158 0.0625 0.125 0.0625 0.25 <1 159 0.0625 0.125 0.0625 0.125 <1 160 0.125 0.25 0.125 0.25 <1 161 0.125 0.125 0.125 0.25 1 162 0.125 0.5 0.25 0.25 <1 163 0.125 0.25 0.125 0.25 1 164 0.5 0.5 0.5 1 <1 165 0.25 0.25 1 0.5 <1 166 0.125 0.125 0.0625 0.25 <1 167 0.0625 0.125 0.0625 0.25 <1 168 0.0625 0.125 0.125 0.25 <1 169 0.25 0.5 0.25 0.25 <1 170 0.125 0.5 0.25 0.5 <1 171 0.125 0.125 0.0625 0.25 <1 172 0.125 0.125 0.125 0.25 <1 173 0.125 0.125 0.0625 0.5 <1 174 0.0625 0.0625 0.0625 0.125 <1 175 0.0625 0.125 0.125 0.125 1 176 0.0625 0.125 0.125 0.125 <1 177 0.0625 0.25 0.0625 0.125 <1 178 0.125 0.125 0.0625 0.125 <1 179 0.125 0.25 0.0625 0.25 <1 180 0.125 0.5 0.25 0.125 <1 181 0.25 0.5 0.25 0.5 <1 182 0.03125 0.125 0.0625 0.125 <1 183 0.125 0.25 0.25 0.125 <1 184 0.125 0.25 0.125 0.25 <1 185 0.125 0.125 0.125 0.125 <1 186 0.125 0.125 0.0625 0.125 <1 187 0.125 0.25 0.5 0.5 <1 188 0.0625 0.25 0.125 0.5 <1 189 0.125 0.125 0.125 0.25 <1 190 0.0625 0.125 0.0625 0.25 <1 191 0.125 0.25 0.125 0.25 1 192 0.25 0.5 0.5 0.5 <1 193 0.125 0.25 0.0625 0.25 <1 194 0.0625 0.0625 0.0625 0.125 <1 195 0.0625 0.125 0.0625 0.125 <1 196 0.25 0.25 0.125 0.25 <1 197 0.0625 0.125 0.0625 0.125 <1 198 0.0625 0.125 0.0625 0.25 <1 199 0.125 0.125 0.0625 0.25 <1 200 0.125 0.5 0.25 0.25 <1 201 0.0625 0.125 0.125 0.125 <1 202 0.125 0.125 0.125 0.125 <1 203 0.0625 0.125 0.0625 0.25 <1 204 0.0625 0.125 0.0625 0.125 1 205 0.25 0.25 0.25 0.25 <1 206 0.03125 0.0625 0.0625 0.125 1 207 0.125 0.125 0.0625 0.125 1 208 0.125 0.125 0.125 0.125 2 209 0.125 0.25 0.25 0.5 <1 210 0.125 0.25 0.25 0.25 <1 211 0.0625 0.0625 0.03125 0.125 <1 212 0.0625 0.25 0.125 0.25 1 213 0.125 0.125 0.0625 0.25 <1 214 0.0625 0.25 0.125 0.5 <1 215 0.125 0.25 0.125 0.25 3 216 0.5 1 1 2 <1 217 0.25 0.5 2 2 <1 218 0.125 0.125 0.125 0.125 <1 219 0.03125 0.0625 0.03125 0.125 <1 220 0.03125 0.0625 0.03125 0.125 <1 221 0.0625 0.125 0.0625 0.125 2 222 0.03125 0.0625 0.0625 0.125 1 223 0.03125 0.0625 0.03125 0.125 <1 224 0.03125 0.125 0.0625 0.125 1 225 0.0625 0.0625 0.125 0.125 <1 226 0.03125 0.125 0.03125 0.125 1 227 0.03125 0.125 0.03125 0.125 <1 228 0.5 0.25 1 0.25 <1 229 0.125 0.125 0.5 0.5 2 230 0.25 0.5 1 1 <1 232 0.0625 0.125 0.0625 0.125 <1 233 0.03125 0.0625 0.0625 0.125 <1 234 0.125 0.25 0.25 0.5 9 235 0.0625 0.25 0.0625 0.25 4 236 0.25 0.25 0.25 0.25 <1 237 0.0625 0.0625 0.03125 0.125 <1 238 0.0625 0.125 0.03125 0.125 2 239 0.125 0.125 0.0625 0.25 1 240 0.0625 0.125 0.03125 0.25 1 241 0.125 0.125 0.125 0.25 <1 242 0.0625 0.125 0.125 0.125 <1 243 0.0625 0.0625 0.0625 0.25 <1 244 0.03125 0.0625 0.03125 0.25 1 245 0.0625 0.125 0.03125 0.25 1 246 0.25 0.25 0.5 0.25 <1 247 0.125 0.25 0.125 0.25 <1 248 0.125 0.125 0.5 0.25 <1 249 0.03125 0.0625 0.03125 0.125 2 250 0.03125 0.0625 0.03125 0.125 1 251 0.03125 0.03125 0.015625 0.0625 1 252 0.0625 0.03125 0.0625 0.0625 2 253 0.03125 0.0625 0.03125 0.0625 2 254 0.03125 0.03125 0.03125 0.0625 1 255 0.0625 0.03125 0.03125 0.0625 1 256 0.03125 0.03125 0.03125 0.0625 1 257 0.03125 0.03125 0.03125 0.0625 1 258 0.0625 0.03125 0.03125 0.0625 2 259 0.015625 0.03125 0.015625 0.0625 2 260 0.015625 0.0625 0.015625 0.0625 <1 261 0.03125 0.0625 0.03125 0.125 1 262 0.03125 0.03125 0.0625 0.125 1 263 0.03125 0.03125 0.03125 0.125 1 264 0.03125 0.125 0.0625 0.25 <1 265 0.0625 0.0625 0.0625 0.125 <1 266 0.03125 0.0625 0.0625 0.125 1 267 0.03125 0.0625 0.0625 0.0625 <1 268 0.0625 0.0625 0.03125 0.125 <1 269 0.015625 0.0625 0.015625 0.0625 <1 270 0.0625 0.0625 0.0625 0.125 <1 271 0.03125 0.0625 0.03125 0.0625 <1 272 0.0625 0.0625 0.0625 0.125 <1 273 0.0625 0.125 0.0625 0.0625 <1 274 0.015625 0.03125 0.03125 0.0625 <1 275 0.0625 0.0625 0.0625 0.125 <1 276 0.03125 0.0625 0.03125 0.0625 <1 277 0.0625 0.125 0.0625 0.125 <1 278 0.03125 0.125 0.0625 0.0625 1 279 0.0625 0.125 0.125 0.125 <1 280 0.03125 0.0625 0.0625 0.125 <1 281 0.03125 0.125 0.0625 0.125 <1 282 0.03125 0.0625 0.015625 0.0625 <1 283 0.0625 0.0625 0.0625 0.125 <1 284 0.0625 0.0625 0.0625 0.125 <1 285 0.0625 0.0625 0.125 0.25 <1 286 0.0625 0.0625 0.125 0.25 <1 287 0.0625 0.0625 0.0625 0.25 <1 288 0.0625 0.125 0.25 0.25 <1 289 0.03125 0.0625 0.03125 0.125 <1 290 0.0625 0.125 0.125 0.25 <1 291 0.0625 0.125 0.25 0.25 <1 292 0.0625 0.25 0.125 0.125 <1 293 0.0625 0.0625 0.0625 0.25 <1 294 0.0625 0.0625 0.0625 0.25 <1 295 0.0625 0.0625 0.0625 0.125 <1 296 0.125 0.0625 0.125 0.25 <1 297 0.03125 0.0625 0.03125 0.125 <1 298 0.03125 0.0625 0.0625 0.25 <1 299 0.0625 0.0625 0.0625 0.25 <1 300 0.125 0.0625 0.125 0.125 <1 301 0.0625 0.125 0.0625 0.125 2 302 0.0625 0.125 0.125 0.125 3 303 0.0625 0.0625 0.25 0.25 <1 304 0.125 0.0625 0.25 0.25 <1 305 0.0625 0.0625 0.0625 0.125 3 306 0.03125 0.0625 0.0625 0.0625 <1 307 0.125 0.125 0.25 0.125 <1 308 0.0625 0.25 0.125 0.125 <1 309 0.015625 0.0625 0.0625 0.125 <1 310 0.03125 0.0625 0.0625 0.125 <1 311 0.0625 0.0625 0.0625 0.25 <1 312 0.03125 0.0625 0.03125 0.125 <1 313 0.015625 0.0625 0.03125 0.125 <1 314 0.015625 0.125 0.015625 0.25 2 315 0.015625 0.0625 0.015625 0.0625 2 316 0.015625 0.0625 0.015625 0.0625 <1 317 0.015625 0.125 0.015625 0.125 <1 318 0.015625 0.0625 0.03125 0.125 1 319 0.0625 0.25 0.125 0.125 <1 320 0.0625 0.125 0.5 0.25 <1 321 0.0625 0.125 0.125 0.125 0 322 0.0625 0.125 0.0625 0.125 <1 323 0.0625 0.125 0.0625 0.125 <1 324 0.0625 0.0625 0.0625 0.0625 <1 325 0.0625 0.0625 0.0625 0.125 <1 326 0.0625 0.0625 0.0625 0.0625 <1 327 0.0625 0.0625 0.0625 0.125 <1 328 0.015625 0.125 0.015625 0.0625 1 329 0.0625 0.125 0.0625 0.125 <1 330 0.0625 0.0625 0.25 0.25 1 331 0.0625 0.0625 0.125 0.125 <1 332 0.03125 0.0625 0.0625 0.25 2 333 0.0625 0.0625 0.125 0.25 2 334 0.03125 0.0625 0.03125 0.125 <1 335 0.0625 0.0625 0.0625 0.125 <1 336 0.0625 0.25 0.0625 0.125 <1 337 0.0625 0.125 0.125 0.25 2 338 0.03125 0.03125 0.03125 0.125 <1 339 0.0625 0.0625 0.0625 0.125 <1 340 0.03125 0.0625 0.0625 0.25 <1 341 0.0625 0.0625 0.0625 0.125 <1 342 0.0625 0.0625 n.d. 0.0625 n.d. 343 0.03125 0.0625 0.0625 0.125 <1 344 0.0625 0.0625 0.125 0.125 <1 345 0.0625 0.0625 0.0625 0.125 <1 346 0.0625 0.0625 0.0625 0.125 <1 347 0.0625 0.0625 0.125 0.125 <1 348 0.0625 0.0625 0.125 0.125 <1 349 0.0625 0.125 0.0625 0.125 <1 350 0.03125 0.125 0.03125 0.125 <1 351 0.0625 0.0625 0.0625 0.125 <1 352 0.125 0.125 1 0.25 <1 353 0.125 0.125 1 0.25 <1 354 0.0625 0.0625 0.03125 0.125 1 355 0.03125 0.0625 0.03125 0.125 6 356 0.0625 0.0625 0.0625 0.125 2 357 0.0625 0.125 0.0625 0.25 <1 358 0.03125 0.125 0.03125 0.125 1 359 0.0625 0.125 0.0625 0.125 1 360 0.0625 0.0625 0.0625 0.125 2 361 0.0625 0.0625 0.0625 0.125 <1 362 0.0625 0.0625 0.0625 0.125 2 363 0.0625 0.0625 0.0625 0.125 2 364 0.0625 0.0625 0.0625 0.125 <1 365 0.03125 0.0625 0.0625 0.125 <1 366 0.125 0.25 0.25 0.25 4 367 0.015625 0.03125 0.007813 0.0625 <1 368 0.015625 0.03125 0.007813 0.0625 1 369 0.015625 0.03125 0.007813 0.0625 <1 370 0.0625 0.0625 0.0625 0.125 2 371 0.0625 0.0625 0.0625 0.0625 0 372 0.0625 0.0625 0.03125 0.0625 <1 373 0.0625 0.0625 0.03125 0.0625 <1 374 0.0625 0.0625 0.0625 0.125 <1 375 0.03125 0.0625 0.03125 0.125 <1 376 0.0625 0.0625 0.0625 0.125 <1 377 0.015625 0.03125 0.015625 0.0625 <1 378 0.0625 0.0625 0.03125 0.0625 <1 379 0.03125 0.0625 0.0625 0.125 <1 380 0.03125 0.0625 0.0625 0.125 <1 381 0.0625 0.0625 0.0625 0.125 <1 382 0.0625 0.0625 0.0625 0.125 <1 383 0.03125 0.0625 0.0625 0.125 <1 384 0.125 0.25 1 0.5 <1 385 0.015625 0.0625 0.03125 0.125 <1 n.d.: not determined

    TABLE-US-00005 TABLE 4 Minimal inhibitory concentrations (MIC) of selected clinical isolates of Escherichia coli, Klebsiella pneumonia, Acintobacter baumannii and Enterobacter cloacae in Mueller-Hinton II broth Escherichia Klebsiella Acinetobacter Enterobacter coli pneumoniae baumannii cloacae 926415 968733 872842 848840 MIC MIC MIC MIC Ex. [μg/mL] [μg/mL] [μg/mL] [μg/mL] 1 1 2 1 4 2 0.125 0.25 0.125 0.5 3 0.25 0.25 0.125 2 4 0.25 0.5 0.125 0.25 5 0.125 0.25 0.125 0.125 6 0.5 0.5 4 4 7 0.5 0.25 1 2 8 0.5 0.25 0.0625 0.25 9 1 0.5 0.125 0.25 10 8 0.5 0.125 0.25 11 4 4 8 2 12 1 4 1 0.5 15 0.25 0.25 0.25 0.125 16 0.25 0.125 0.25 0.25 17 0.5 0.5 0.125 0.25 18 0.25 0.5 0.25 0.125 20 1 2 0.5 0.25 21 8 8 2 0.5 22 0.5 1 0.25 0.125 23 0.5 0.5 0.25 0.125 24 2 0.5 1 0.25 25 0.25 0.25 0.25 0.125 26 0.125 0.25 0.125 0.25 27 1 1 0.125 0.25 28 8 8 4 0.125 29 4 8 1 0.0625 31 0.5 0.125 0.125 0.125 32 0.0625 0.25 0.0625 0.125 33 0.125 0.25 0.0625 0.125 34 0.0625 0.125 0.0625 0.125 35 1 0.25 0.25 0.25 36 0.125 0.25 0.0625 0.125 37 0.5 2 1 0.25 38 0.5 0.25 0.25 0.5 39 0.25 0.5 0.25 0.5 40 1 0.25 0.5 0.5 41 0.25 0.125 0.125 0.25 42 0.5 2 1 4 43 0.5 2 0.125 2 44 0.125 0.25 0.125 0.125 45 0.5 0.5 0.25 0.25 46 0.125 0.5 0.125 0.125 47 0.25 1 0.125 4 48 1 8 0.5 4 49 0.25 0.125 0.25 0.25 50 0.5 4 1 8 51 0.5 1 0.25 0.5 52 2 4 2 2 53 0.5 4 0.5 8 54 0.5 4 0.5 4 55 1 8 1 8 57 0.5 4 0.5 0.25 58 0.125 0.25 0.0625 0.125 59 0.125 0.25 0.25 1 60 0.125 0.125 0.125 4 61 0.25 0.125 0.125 0.125 62 0.25 0.125 0.125 4 63 0.5 0.25 0.25 4 64 0.5 1 0.5 4 65 0.5 0.5 0.25 4 66 1 4 0.5 0.5 67 2 2 2 2 68 2 1 8 n.d. 69 0.0625 0.125 0.0625 0.125 70 0.5 0.25 0.25 0.125 71 0.25 0.25 0.125 0.25 72 0.125 0.125 0.0625 0.25 73 0.125 0.125 0.0625 0.125 74 0.25 0.0625 0.0625 0.125 75 0.125 0.125 0.0625 0.125 76 0.125 0.125 0.25 0.125 77 0.25 0.25 0.25 0.25 78 0.125 0.0625 0.125 2 79 0.0625 0.0625 0.0625 0.0625 80 0.0625 0.125 0.0625 0.125 81 0.125 0.125 0.25 0.125 82 0.5 0.25 0.25 0.25 83 0.25 0.25 0.125 0.125 84 0.125 0.125 0.125 0.25 85 0.25 0.25 0.25 0.125 86 0.25 0.125 0.25 1 87 0.0625 0.125 0.25 2 88 0.125 0.125 0.125 0.125 89 0.5 1 0.5 0.5 90 0.5 0.25 0.125 0.25 91 2 2 0.5 1 92 0.0625 0.125 0.125 0.25 93 0.25 0.5 0.5 0.25 94 0.25 0.25 0.25 1 95 0.125 0.125 0.125 4 96 0.5 0.125 0.5 8 97 2 8 2 n.d. 98 2 4 2 2 99 0.125 0.0625 0.0625 0.125 100 0.25 0.0625 0.125 0.125 101 0.5 0.5 0.125 0.25 102 2 4 0.5 0.5 103 0.125 0.25 0.0625 0.125 104 0.0625 0.0625 0.0625 0.125 105 0.25 0.25 0.125 0.125 106 0.125 0.25 0.25 0.25 107 0.125 0.125 0.0625 0.0625 108 0.125 0.125 0.0625 0.125 109 0.0625 0.125 0.0625 0.125 110 0.125 0.125 0.0625 0.0625 111 0.0625 0.125 0.0625 0.125 112 0.0625 0.125 0.0625 0.125 113 0.25 0.5 0.25 0.125 114 0.0625 0.0625 0.03125 0.0625 115 0.125 0.25 0.125 0.0625 116 0.125 0.25 0.0625 0.03125 117 0.0625 0.0625 0.015625 0.0625 119 0.0625 0.125 0.03125 0.0625 120 0.0625 0.125 0.0625 0.25 121 0.125 0.25 0.0625 0.125 122 4 2 1 2 123 0.03125 0.0625 0.03125 0.0625 124 0.25 0.25 0.0625 0.125 125 0.0625 0.125 0.125 0.125 126 0.125 0.25 0.25 0.5 127 0.125 0.5 0.0625 0.125 128 0.125 0.0625 0.0625 0.0625 129 0.25 0.125 0.125 0.125 130 0.125 0.125 0.125 0.0625 131 0.5 1 1 0.25 132 0.0625 0.125 0.0625 0.125 133 0.0625 0.125 0.03125 0.25 134 0.125 0.125 0.0625 0.125 135 0.0625 0.125 0.03125 0.0625 136 0.0625 0.0625 0.03125 0.0625 137 0.125 0.125 0.125 0.0625 138 0.03125 0.0625 0.03125 0.125 139 0.125 0.25 0.0625 0.125 140 0.25 0.5 0.5 0.25 141 0.03125 0.03125 0.0625 0.0625 142 0.03125 0.0625 0.03125 0.125 143 0.125 0.0625 0.03125 0.0625 144 0.0625 0.0625 0.0625 0.125 145 0.0625 0.125 0.03125 0.125 146 0.25 0.25 0.125 0.25 147 0.25 0.5 0.25 0.125 148 0.125 0.25 0.0625 0.0625 149 0.25 0.5 0.125 0.125 150 0.25 0.5 0.125 0.125 151 0.5 1 0.25 0.125 152 2 8 1 0.5 153 0.125 0.25 0.0625 0.125 154 0.125 0.25 0.0625 0.125 155 0.5 0.5 0.125 0.125 156 0.125 0.25 0.125 0.125 157 1 1 0.5 0.25 158 0.5 1 0.25 0.125 159 0.25 0.5 0.25 0.125 160 0.5 0.5 0.5 2 161 0.5 0.25 0.25 1 162 1 8 0.5 n.d. 163 0.5 0.5 0.25 4 164 0.25 1 2 n.d. 165 0.125 0.5 1 4 166 0.25 0.125 0.25 0.25 167 0.25 0.25 0.125 2 168 0.125 0.5 0.125 0.25 169 0.5 4 1 n.d. 170 0.5 2 2 n.d. 171 0.125 0.5 0.0625 0.5 172 0.25 0.5 0.125 0.25 173 0.25 2 0.125 4 174 0.125 0.25 0.125 0.25 175 0.25 0.5 0.0625 0.25 176 0.25 0.25 0.125 0.5 177 0.25 0.5 0.125 1 178 0.5 2 0.25 0.25 179 0.5 4 0.25 0.5 181 2 8 2 1 182 0.5 1 0.125 0.125 184 2 8 1 1 185 0.25 1 0.25 0.25 186 1 8 0.25 0.25 188 0.5 1 0.5 0.5 189 1 4 0.5 0.25 190 1 4 0.5 0.5 191 1 2 0.5 0.5 193 0.5 0.5 0.5 0.5 194 0.5 0.25 0.25 0.125 195 0.5 0.5 0.25 0.25 196 2 2 1 1 197 0.5 0.5 0.25 0.25 198 0.25 0.5 0.125 0.25 199 0.5 0.5 0.25 0.25 200 2 2 1 2 201 0.25 0.25 0.125 0.125 202 0.25 0.25 0.25 0.125 203 0.5 0.25 0.125 0.5 204 0.5 0.5 0.25 0.125 206 0.0625 0.5 0.0625 0.125 207 0.5 1 0.25 0.5 208 0.25 0.5 0.125 0.25 209 1 4 2 n.d. 210 2 2 0.5 2 211 0.25 0.25 0.0625 2 212 1 2 0.5 0.5 213 0.5 0.5 0.125 1 214 0.5 0.5 0.5 8 215 2 2 0.5 0.5 216 1 4 2 n.d. 217 1 2 4 n.d. 219 0.25 0.5 0.125 0.125 220 0.125 0.125 0.0625 0.125 221 0.125 0.25 0.0625 0.125 222 0.25 0.25 0.0625 0.125 223 0.125 0.25 0.03125 0.0625 224 0.125 0.25 0.0625 0.125 225 0.25 1 0.25 0.125 226 0.0625 0.25 0.0625 0.0625 227 0.125 0.5 0.125 0.125 228 1 1 4 8 232 0.0625 0.125 0.0625 0.125 233 0.0625 0.0625 0.0625 0.125 234 0.25 1 0.25 0.5 235 0.125 0.25 0.0625 0.25 236 2 8 2 1 237 0.25 0.5 0.125 0.125 238 0.125 0.25 0.0625 0.125 239 0.0625 0.25 0.125 0.25 240 0.0625 0.5 0.0625 0.125 241 1 1 0.125 2 242 0.25 1 0.125 4 243 0.125 0.125 0.0625 0.25 244 0.125 0.0625 0.0625 0.0625 245 0.125 0.25 0.0625 0.125 246 2 4 4 2 247 0.5 8 0.5 0.25 248 0.25 4 1 4 249 0.125 0.25 0.03125 0.125 250 0.0625 0.125 0.03125 0.0625 251 0.125 0.0625 0.03125 0.125 252 0.125 0.125 0.0625 0.125 253 0.0625 0.0625 0.03125 0.125 254 0.125 0.125 0.03125 0.0625 255 0.0625 0.25 0.125 0.0625 256 0.0625 0.0625 0.03125 0.0625 257 0.0625 0.125 0.03125 0.0625 258 0.25 0.125 0.03125 0.0625 259 0.125 0.0625 0.03125 0.0625 260 0.5 0.5 0.0625 0.0625 261 0.125 0.25 0.0625 0.125 262 0.25 0.25 0.0625 0.0625 263 0.125 0.25 0.0625 0.125 264 0.125 0.125 0.0625 0.5 265 0.125 0.25 0.125 0.5 266 0.5 1 0.5 0.25 267 0.0625 0.125 0.0625 0.125 268 0.5 0.5 0.125 0.25 269 0.0625 0.0625 0.03125 0.125 270 0.125 0.125 0.0625 0.25 271 0.0625 0.0625 0.0625 0.25 272 0.125 0.125 0.0625 0.25 273 0.5 0.5 0.0625 0.25 274 0.125 0.125 0.125 0.25 275 0.125 0.25 0.125 1 276 0.25 0.25 0.0625 0.125 277 0.25 0.25 0.125 0.125 278 0.25 0.25 0.125 0.125 279 1 2 0.5 0.25 280 0.25 0.5 0.125 0.0625 281 0.25 0.25 0.25 0.125 282 0.125 0.25 0.125 0.0625 283 0.5 2 0.5 0.125 284 1 2 0.5 0.125 285 2 4 0.5 0.25 286 1 2 0.5 0.25 287 1 2 0.25 0.125 288 4 8 1 1 289 0.25 0.25 0.0625 0.125 290 1 4 0.25 0.25 291 2 8 1 1 292 1 4 0.5 1 293 0.5 2 0.5 0.5 294 0.25 1 0.5 0.125 295 0.5 0.5 0.125 0.25 296 0.5 4 0.25 0.5 297 0.125 0.125 0.0625 0.125 298 0.5 1 0.25 0.25 299 0.25 0.5 0.125 0.125 300 0.25 2 1 0.125 301 0.125 0.5 0.25 0.125 302 2 2 0.5 0.5 303 1 1 0.5 1 304 2 4 1 2 305 0.25 0.25 0.125 0.25 306 0.0625 0.125 0.0625 0.0625 307 0.5 1 0.5 4 308 0.5 1 0.5 1 309 0.0625 0.125 0.03125 0.0625 310 0.0625 0.0625 0.0625 0.0625 311 0.25 0.125 0.125 0.125 312 0.25 0.125 0.0625 0.0625 313 0.125 0.125 0.125 0.0625 314 0.0625 0.125 0.0625 0.125 315 0.0625 0.0625 0.0625 0.125 316 0.0625 0.0625 0.03125 0.0625 317 0.0625 0.125 0.03125 0.0625 318 0.125 0.125 0.0625 0.125 319 1 4 0.5 1 320 4 8 1 2 321 0.5 1 0.25 0.25 322 0.125 0.25 0.0625 0.0625 323 0.25 0.5 0.0625 0.125 324 0.125 0.5 0.125 0.125 325 0.125 0.5 0.125 0.0625 326 0.125 0.5 0.125 0.0625 327 0.25 0.5 0.125 0.125 328 0.125 0.25 0.0625 0.0625 329 0.125 0.25 0.125 0.125 330 0.25 2 1 0.125 331 0.5 0.5 0.25 0.25 332 0.25 0.5 0.25 0.125 333 0.5 1 0.5 0.25 334 0.25 0.25 0.125 0.125 335 0.25 0.5 0.25 0.25 336 0.5 0.5 0.125 0.125 337 1 2 0.25 0.25 338 0.0625 0.125 0.0625 0.0625 339 0.5 0.5 0.125 0.125 340 0.125 0.25 0.0625 0.125 341 0.5 1 0.25 2 342 0.125 0.25 0.0625 343 0.25 0.5 0.25 0.125 344 0.125 0.25 0.25 1 345 0.125 0.25 0.125 0.125 346 0.25 0.5 0.125 0.125 347 0.25 1 0.25 0.5 348 0.5 2 0.5 0.5 349 0.25 0.25 0.25 0.25 350 0.125 0.125 0.0625 0.125 351 0.5 1 0.25 0.25 352 0.25 0.5 4 8 353 0.25 4 4 8 354 0.5 0.25 0.0625 0.125 355 0.25 0.25 0.0625 0.125 356 0.25 0.25 0.125 0.125 357 0.5 0.5 0.25 0.125 358 0.25 0.25 0.0625 0.125 359 0.25 0.5 0.125 0.125 360 0.25 0.5 0.125 0.125 361 0.125 0.125 0.0625 0.0625 362 0.0625 0.125 0.0625 0.0625 363 0.125 0.125 0.0625 0.0625 364 0.25 0.125 0.125 0.125 365 0.125 0.125 0.0625 0.0625 366 0.5 2 0.5 8 367 0.0625 0.0625 0.03125 0.0625 368 0.015625 0.0625 0.03125 0.03125 369 0.0625 0.0625 0.03125 0.03125 370 0.5 1 0.5 0.125 371 0.25 0.5 0.0625 0.5 372 0.125 0.25 0.125 0.25 373 0.125 0.125 0.0625 0.25 374 0.5 1 0.25 0.25 375 0.125 0.125 0.0625 0.25 376 0.25 0.5 0.25 0.0625 377 0.125 0.0625 0.0625 0.0625 378 0.0625 0.125 0.0625 0.0625 379 0.25 0.25 0.125 1 380 0.125 0.5 0.25 0.125 381 0.5 1 0.25 0.5 382 0.125 0.25 0.25 0.125 383 0.25 1 0.125 0.125 384 4 >8 2 2 385 0.0625 0.125 0.0625 0.0625 Colistin .sup.1) 3) 16 16 64 >8 Colistin .sup.2) 3) 8 >8 >8 >8 .sup.1) measured in absence of P-80 .sup.2) measured in presence of P-80 .sup.3) Colistin (Colistin sulfate salt, Cat-Nr. C4461, Lot-Nr. SLBK0713V) obtained from Sigma Aldrich, Buchs; Switzerland

    TABLE-US-00006 TABLE 5 Minimal inhibitory concentrations (MIC) of Escherichia coli MCR-1 Af45 in Mueller-Hinton II broth Escherichia coli MCR-1 Af45 Ex. MIC [μg/mL] 3 0.125 41 0.125 72 0.125 73 0.125 79 0.125 84 0.125 88 0.25 92 0.25 96 0.25 99 0.0625 100 0.125 103 0.0625 104 0.125 105 0.5 106 0.25 107 0.125 108 0.0625 109 0.125 110 0.125 111 0.125 112 0.125 113 0.5 114 0.0625 115 0.25 116 0.25 117 0.125 119 0.125 120 0.25 126 0.5 128 0.25 129 0.125 132 0.125 133 0.125 134 0.25 135 0.125 136 0.125 137 0.25 138 0.125 139 0.25 140 0.25 141 0.0625 142 0.125 143 0.5 144 0.125 145 0.25 147 0.5 148 0.25 150 0.25 151 0.5 153 0.25 154 0.125 156 0.25 159 0.25 161 0.25 166 0.25 168 0.25 172 0.125 185 0.5 193 0.5 199 0.5 201 0.125 202 0.25 203 0.25 204 0.25 206 0.25 219 0.25 221 0.25 222 0.5 223 0.25 224 0.5 225 0.25 226 0.25 232 0.0625 233 0.125 250 0.125 276 0.25 281 0.125 282 0.25 289 0.25 297 0.125 310 0.0625 334 0.125 340 0.0625 341 0.5 350 0.25 351 0.25 359 0.125 365 0.0625 375 0.125 379 0.125 Colistin .sup.1) 3) 4 Colistin .sup.2) 3) 2 .sup.1) measured in absence of P-80 .sup.2) measured in presence of P-80 .sup.3) Colistin (Colistin sulfate salt, Cat-Nr. C4461, Lot-Nr. SLBK0713V) obtained from Sigma Aldrich, Buchs; Switzerland

    TABLE-US-00007 TABLE 6 Tolerability in a mouse model Ex. Mortality and dose 39 0/3 died at 2 × 30 mg/kg 41 0/3 died at 2 × 30 mg/kg 42 0/3 died at 2 × 30 mg/kg 43 0/3 died at 2 × 30 mg/kg 58 0/3 died at 2 × 30 mg/kg 65 0/3 died at 2 × 30 mg/kg 92 0/3 died at 2 × 30 mg/kg 96 0/3 died at 2 × 30 mg/kg 100 0/3 died at 2 × 30 mg/kg 114 0/3 died at 2 × 30 mg/kg 115 0/3 died at 2 × 30 mg/kg 116 0/3 died at 2 × 30 mg/kg 137 0/3 died at 2 × 30 mg/kg 150 0/3 died at 2 × 30 mg/kg 161 0/3 died at 2 × 30 mg/kg 188 0/3 died at 2 × 30 mg/kg 215 0/3 died at 2 × 30 mg/kg 219 0/3 died at 2 × 30 mg/kg 257 0/3 died at 2 × 30 mg/kg 258 0/3 died at 2 × 30 mg/kg 259 0/3 died at 2 × 30 mg/kg 260 0/3 died at 2 × 30 mg/kg 261 0/3 died at 2 × 30 mg/kg 266 0/3 died at 2 × 30 mg/kg 270 0/3 died at 2 × 40 mg/kg 274 0/3 died at 2 × 40 mg/kg 275 0/3 died at 2 × 40 mg/kg 276 0/3 died at 2 × 40 mg/kg 277 0/3 died at 2 × 40 mg/kg 278 0/3 died at 2 × 40 mg/kg 279 0/3 died at 2 × 40 mg/kg 280 0/3 died at 2 × 40 mg/kg 281 0/3 died at 2 × 40 mg/kg 282 0/3 died at 2 × 40 mg/kg 283 0/3 died at 2 × 40 mg/kg 284 0/3 died at 2 × 40 mg/kg 289 0/3 died at 2 × 40 mg/kg 293 0/3 died at 2 × 40 mg/kg 294 0/3 died at 2 × 40 mg/kg 295 0/3 died at 2 × 40 mg/kg 296 0/3 died at 2 × 40 mg/kg 297 0/3 died at 2 × 40 mg/kg 298 0/3 died at 2 × 40 mg/kg 299 0/3 died at 2 × 40 mg/kg 300 0/3 died at 2 × 40 mg/kg 306 0/3 died at 2 × 40 mg/kg 309 0/3 died at 2 × 40 mg/kg 310 0/3 died at 2 × 40 mg/kg 311 0/3 died at 2 × 40 mg/kg 331 0/3 died at 2 × 40 mg/kg 332 0/3 died at 2 × 40 mg/kg 333 0/3 died at 2 × 40 mg/kg 334 0/3 died at 2 × 40 mg/kg 335 0/3 died at 2 × 40 mg/kg 336 0/3 died at 2 × 40 mg/kg 337 0/3 died at 2 × 40 mg/kg 338 0/3 died at 2 × 40 mg/kg 339 0/3 died at 2 × 40 mg/kg 340 0/3 died at 2 × 40 mg/kg 341 0/3 died at 2 × 40 mg/kg 343 0/3 died at 2 × 40 mg/kg 344 0/3 died at 2 × 40 mg/kg 345 0/3 died at 2 × 40 mg/kg 350 0/3 died at 2 × 40 mg/kg 351 0/3 died at 2 × 40 mg/kg 358 0/3 died at 2 × 40 mg/kg 359 0/3 died at 2 × 40 mg/kg 361 0/3 died at 2 × 40 mg/kg 362 0/3 died at 2 × 40 mg/kg 363 0/3 died at 2 × 40 mg/kg 364 0/3 died at 2 × 40 mg/kg 365 0/3 died at 2 × 40 mg/kg 370 0/3 died at 2 × 40 mg/kg 375 0/3 died at 2 × 40 mg/kg 376 0/3 died at 2 × 40 mg/kg 379 0/3 died at 2 × 40 mg/kg 380 0/3 died at 2 × 40 mg/kg 381 0/3 died at 2 × 40 mg/kg 382 0/3 died at 2 × 40 mg/kg 383 0/3 died at 2 × 40 mg/kg

    TABLE-US-00008 TABLE 7 Nephrotoxicity in a mouse model Max Overall Kidney Histology Semi-Quantiative Ex. Score Score (SQS) 39 1 +1 100 2 +1 113 3 +1 114 6 +1 115 4 +1 128 12 +1 132 12 +1 137 1 +1 260 3 +1 276 2 +1 277 2 +1 278 2 +1 279 1 +1 281 2 +1 282 2 +1 289 0 0 293 1 +1 297 1 +1 306 3 +1 310 2 +1 334 2 +1 340 3 +1 341 2 +1 350 8 +1 351 3 +1 Colistin B 24 +2