A method for generating a dimerization and/or degradation moiety for a first protein and a second protein, where the method includes (a) generating, in silico a set of poses by docking a first protein, and a second protein, (b) generating a subset of poses by selecting one or more poses from the set of poses based on the scores of the poses, (c) identifying a candidate pose from the subset of poses based on the spatial relationship between the two proteins, (d) designing a linker between the first ligand and the second ligand that accommodates the candidate pose, and (e) synthesizing or having synthesized the dimerization and/or degradation moiety having the first ligand, the second ligand, and the linker.

The invention discloses a method for the preparation of a peptide by liquid phase coupling of two fragments, an N-terminal fragment and a C-terminal fragment of the desired peptide, wherein the C-terminal fragment is protected on its C-terminal COOH by a psWang linker; the method is demonstrated with liraglutide wherein the C-terminal fragment carries the Palmitoyl-Glu-OtBu residue on the Lys.

A method of downstream purification of a recombinant protein in fusion with a hydrophobin-intein tag using alcohol precipitation. The method comprises (1) constructing a plasmid expressing a fusion protein in a host cell, wherein the fusion protein includes a target protein domain, an intein, and a hydrophobin domain; (2) culturing the host cell transfected with the plasmid forming a cell culture medium; (3) separating a cell culture supernatant containing the fusion protein from the cell culture medium; and (4) purifying a substantial amount of the target protein from the cell culture supernatant without its hydrophobin-intein fusion tag using alcohol precipitation.

A method for synthesizing a peptide having the sequence His-X-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Y-Glu-Phe-Ile-Ala-Trp-Leu-Val-Z-Gly-Arg-Gly is disclosed. The method includes enzymatically coupling: (a) a peptide C-terminal ester or thioester having a first peptide fragment with the sequence His-X-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-(thio)ester; and (b) a peptide nucleophile having an N-terminally unprotected amine having a second peptide fragment with the sequence H-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Y-Glu-Phe-Ile-Ala-Trp-Leu-Val-Z-Gly-Arg-Gly; wherein: X is Ala or an ?-amino-isobutyric acid (Aib) residue; Y is Lys, which Lys has a free side-chain ?-amino group or of which Lys the side-chain ?-amino group is protected with a protective group or of which Lys the side-chain ?-amino group is functionalized with an amino acid or another functional group; and Z is Arg or Lys.

The invention relates to an improved method for a 5+3+2 solution phase syntheses of Icatibant acetate (1) comprising coupling of suitably protected peptide fragments which on deprotection followed by treatment with acetic acid provide Icatibant acetate (1) having desired purity.

Novel hybrid polymers are disclosed that have a structure represented by the following formula I: ##STR00001##
wherein Abiotic oligomer, Polypeptide, X, Y, and R.sup.1 are as described herein. The methods to prepare the hybrid polymers via novel oxazolidinyl compounds are also described.

The present invention provides methods of making 47 peptide monomer and dimer antagonists. Methods of the present invention include solid phase and solution phase methods, as well as synthesis via condensation of smaller peptide fragments. Methods of the present invention further include methods directed to the synthesis of peptides comprising one or more penicillamine residues.

A production method for an MP whey is provided, that enables preparation of both of a high GMP-content composition and a usable MP whey from an ordinary MP whey. The problems can be solved by a production method for a glycomacropeptide-containing composition, that includes a step of acquiring a solution containing glycomacropeptide, that includes a glycomacropeptide content of 10% by weight or higher in the protein total amount by condensing and/or applying diafiltration to a microparticulated whey solution.

The object of the present invention is to provide a glycosylated polypeptide having uniform sugar chain structure which has interferon activity. It was found that a glycosylated polypeptide having uniform sugar chain structure as well as having interferon activity can be prepared by a method comprising a step of synthesizing a glycosylated peptide fragment and at least two peptide fragments and a step of linking the glycosylated peptide fragment and the at least two peptide fragments.

The invention relates to a subtilisin BPN variant or homolog thereof, having the following mutations compared to subtilisin BPN represented by SEQUENCE ID NO: 2 or a homolog sequence thereof:a deletion of the amino acids corresponding to positions 75-83;a mutation at the amino acid position corresponding to S221, the mutation corresponding to S221C or S221 selenocysteine, preferably S221C;at least one further mutation selected from the group consisting of amino acid positions corresponding to F189W, F189Y, S33D, S33T, N218D, N218T, N218E, N62D, N62S, N62W, and N62Y; preferably a mutation at the amino acid position corresponding to P225; wherein the amino acid positions are defined according to the sequence of subtilisin BPN represented by SEQUENCE ID NO: 2. The invention further relates to enzymatically synthesizing a peptide.