The purpose of the present invention is to provide a protecting group which improves the solubility of a compound having a functional group protected with the protecting group in an organic solvent and which is easily separated and purified after a reaction with avoiding solidification or insolubilization. Provided is a benzyl compound represented by Formula (1) where X.sup.1 represents CH.sub.2OR.sup.14 (where R.sup.14 represents a hydrogen atom, a halogenocarbonyl group, or an active ester-type protecting group), CH.sub.2NHR.sup.15 (where R.sup.15 represents a hydrogen atom, a linear or branched alkyl group having 1 to 6 carbon atoms, or an aralkyl group), a halogenomethyl group, a methyl azide group, a formyl group, or an oxime; and at least one of R.sup.1, R.sup.2, R.sup.3, R.sup.4, and R.sup.5 is a group represented by Formula (2), and the remainders each represent a hydrogen atom, a halogen atom, an alkyl group having 1 to 4 carbon atoms, or an alkoxy group having 1 to 4 carbon atoms, where R.sup.6 represents a linear or branched alkylene group having 1 to 16 carbon atoms; X.sup.2 represents O or CONR.sup.16 (where R.sup.16 represents a hydrogen atom or an alkyl group having 1 to 4 carbon atoms); and A represents a group represented by Formula (3), (4), (5), (6), (7), (8), (9), (10), (11), (12), or (13).

It was found that a salt formed of an acid and a base having characteristics set forth below can inactivate a deprotecting agent, thereby suppressing redundant peptide elongation: (i) the base is different in type from a base used as a deprotecting agent, and (ii) a conjugate acid of the base has a pKa smaller than that of a conjugate acid of a base used as a deprotecting agent.

A method for producing a peptide by conducting steps (1) condensing an N-protected amino acid or an N-protected peptide to an N-terminus of a C-protected amino acid or a C-protected peptide represented by formula (II):

##STR00001##

wherein Y represents an amino acid or a peptide with an unprotected N-terminus; R.sup.1, R.sup.2 and R.sup.3 each independently represent an optionally substituted aliphatic hydrocarbon group, an optionally substituted aromatic hydrocarbon group, or OR.sup.4 (wherein R.sup.4 represents an optionally substituted aliphatic or aromatic hydrocarbon group; two of R.sup.1, R.sup.2 and R.sup.3 may form a 5- to 7-membered ring together with the Si atom to which they are bonded; and the R.sup.1R.sup.2R.sup.3Si group has 8 or more carbon atoms and is bonded to a C-terminus of an amino acid or a peptide in Y, and (2) removing the protective group at the N-terminus of the peptide obtained in step (1).

Methods are disclosed for producing highly purified recombinant human insulin (RHI) having a purity of 99.0% (w/w) or greater, a Total Impurity (not including the related substance desamido Asn.sup.A21-RHI, as specified by USP) of 0.8% (w/w) or less, and an impurity C of 0.1% (w/w) or less. Also disclosed are API compositions of highly purified RHI having a purity of 99.0% (w/w) or greater, a Total Impurity of 0.8% (w/w) or less, and an impurity C of 0.1% (w/w) or less.

Disclosed herein are formulations, substrates, and arrays for amino acid and peptide synthesis on microarrays. In certain embodiments, methods for manufacturing and using the formulations, substrates, and arrays including one-step coupling, e.g., for synthesis of peptides in a C.fwdarw.N orientation are disclosed. In some embodiments, disclosed herein are formulations and methods for high efficiency coupling of biomolecules to a substrate.

The present invention relates to a novel process for the preparation of Pasireotide of formula 11 [Cyclo [Phe-{4-(OCONHCH.sub.2CH.sub.2NH.sub.2)) Pro}-Phg-DTrp-Lys-Tyr(Bzl)]]. The invention also relates to a novel intermediate compound of formula 8 and process thereof which is used for preparation of compound of formula 11. ##STR00001##

The present invention relates to an improved process for the preparation of Cetrorelix acetate (1). More particularly, the present invention relates to the purification of Cetrorelix acetate (1) by simple method.

##STR00001##

The invention relates to methods for synthesizing amanitin derivatives having an amino group attached to position 6 of the central tryptophan moiety. The invention furthermore relates to an amanitin derivative having an amino group attached to position 6 of the central tryptophan moiety, conjugates of such amanitin derivative, and pharmaceutical compositions comprising such conjugates.

To develop a protecting group that facilitates separation and purification, after reaction, of a compound including a protected functional group, without solidifying or insolubilizing the compound. A xanthene compound of by General Formula (1) ##STR00001## (wherein Y is OR.sup.17 (R.sup.17 is a hydrogen atom or an active ester-protecting group), NHR.sup.18 (R.sup.18 is a hydrogen atom, or a linear or branched C.sub.1-C.sub.6 alkyl group or aralkyl group), an azide, a halogen atom, or a carbonyl group formed together with a methylene group; at least one of R.sup.1 to R.sup.8 is represented by Formula (2);
OR.sup.9X-A(2) and a residue is a hydrogen atom, a halogen atom, a C.sub.1-C.sub.4 alkyl group, or a C.sub.1-C.sub.4 alkoxy group, wherein R.sup.9 is a linear or branched C.sub.1-C.sub.16 alkylene group; X is O or CONR.sup.19 (R.sup.19 is a hydrogen atom or a C.sub.1-C.sub.4 alkyl group); and A is represented by Formula (3) or the like ##STR00002## (wherein R.sup.10, R.sup.11, and R.sup.12, the same or different, are a linear or branched C.sub.1-C.sub.6 alkyl group or an aryl group optionally including a substituent; R.sup.13 is a single bond or a linear or branched C.sub.1-C.sub.3 alkylene group; and R.sup.14, R.sup.15, and R.sup.16 are a linear or branched C.sub.1-C.sub.3 alkylene group)).

When the initiation suppression method was used for translation of a peptide having at its N terminus an amino acid residue carrying a thiol group near its amino group with specific protecting groups being introduced to the thiol group and the amino group, it was found that not only the probability of initiation of amino acid translation reaction was improved, but also production of cleaved peptides was suppressed and translation efficiency and purity were improved. Furthermore, it was found that it is possible to efficiently promote the cyclization reaction of the peptide through amide bond formation. Based on these findings, the inventors discovered novel methods for preparing complexes between nucleic acids and peptides containing various unnatural amino acids and having an amide bond-mediated cyclized portion.