An object of the present invention is to provide a novel method having high efficiency and versatility for a peptide thioester and peptide. The present invention provides a method for producing a peptide thioester, comprising the steps of: (1) providing a peptide thioester having a CGC triplet at the C-terminal; (2) causing a transfer between an SH group of the C-terminal cysteine and a carbonyl group of the glycine in the CGC triplet to obtain an R-X-CG-thioester; and (3) causing, in the R-X-CG-thioester, a transfer between the SH group of the cysteine and a carbonyl group of X, and a transfer between an amino group of the cysteine and a thiol group of the glycine to obtain a peptide thioester, and a method for producing a peptide using the peptide thioester produced by this method.

The present invention relates to methods for the enhancement and stabilisation of the proteolytic activity of proteases, methods for producing compositions comprising proteases with proteolytic activity that has been enhanced and stabilised, compositions comprising proteases with proteolytic activity that has been enhanced and stabilised obtained or obtainable by the aforementioned methods, use of such compositions in the manufacture of medicaments and cosmetics, the use of such compositions in the treatment of diseases and disorders including wounds, and in cosmetic applications, and associated kits.

The present disclosure pertains to the field peptide stapling and/or macrocyclization, where a structural motif is used to improve the properties of amino acid sequences (e.g. protease resistance, cellular penetration, biological activity). Also within the scope of the disclosure are methods for unstapling the S,S-tetrazine-containing amino acid sequence. The disclosure is also directed to methods for the reductive removal of thiocyanates from an amino acid sequence with cysteine to recycle back to the native amino acid sequence.

The present invention relates to novel methods of making soluble proteins having free cysteines in which a host cell is exposed to a cysteine blocking agent. The soluble proteins produced by the methods can then be modified to increase their effectiveness. Such modifications include attaching a PEG moiety to form pegylated proteins.

The invention provides improved methods of conjugating an agent to a thiol moiety in a protein that contains at least one disulfide bond and at least one trisulfide bond. Exemplary embodiments include the production of antibody drug conjugates substantially free of impurities created in the presence of reactive sulfide moieties in the production processes.

The present invention provides a novel method for manufacturing a protein, particularly where said protein is to be coupled with another molecule. The invention further provides a method for industrial scale protein manufacturing to obtain proteins, e.g., for therapeutic purposes.

The present invention provides methods of making α4β7 peptide monmer 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.

The present invention provides a method for making uncapped cysteine protein preparations, including uncapped engineered cysteine antibody preparations. The methods include, inter alia, contacting a reducing agent with engineered cysteine antibody molecules, each of the antibody molecules having at least one capped engineered cysteine residue and at least one interchain disulfide bond and reacting the reducing agent with the antibody molecules under conditions sufficient to uncap engineered cysteine residues and form cap byproducts. The method also includes removing the cap byproduct during the reduction reaction. Substantially all of the interchain disulfide bonds present in the antibody molecules prior to reduction are retained following reduction. Antibody conjugates and methods for preparing antibody conjugates using uncapped antibody preparations are also described.

The present application relates to an improved process for the formation of disulfide bonds in linaclotide. The present application also relates to an improved process for the purification of linaclotide.

The subject matter of the invention is a method for conjugation of free thiol group(s) containing biomolecules, leading to the biomolecular complex formation, comprising a reaction to connect biomolecules using a gold-donor agent in which a —S—Au—S— bond is formed, characterised in that a gold-donor agent is halogen(triarylphosphine)gold (I). The subject matter of the invention is also the use of halogen(triarylphosphine)gold (I) molecules as the gold-donor agent in the method of biomolecular complex formation.