An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

A novel method for synthesizing a Hirulog peptide is devised.

A novel method for synthesizing a Hirulog peptide is devised.

The present invention provides composite proteins, including antibodies, which show reduced immunogenicity. In particular, composite antibodies for use in humans are provided, in particular antibodies which have been modified to remove one or more T-cell epitopes. Methods for generating such proteins are also provided.

The present invention provides composite proteins, including antibodies, which show reduced immunogenicity. In particular, composite antibodies for use in humans are provided, in particular antibodies which have been modified to remove one or more T-cell epitopes. Methods for generating such proteins are also provided.

A method of purifying a fusion protein, including: (1) adjusting the pH of an aqueous phase, containing a fusion protein which is a fusion of a protein having a self-assembly capability and a tamet protein, and which aqueous phase has a first pH, to a second pH, to obtain a remaining aqueous phase and a solid fraction containing an amount of the fusion protein; (2) separating the solid fraction from the remaining aqueous phase, to obtain a separated solid fraction; and (3) dissolving the separated solid fraction in a solution having a pH of 12 or lower but higher than the second pH by at least 0.1 pH units, wherein the protein having a self-assembly capability is a cell surface protein.

A method of purifying a fusion protein, including: (1) adjusting the pH of an aqueous phase, containing a fusion protein which is a fusion of a protein having a self-assembly capability and a tamet protein, and which aqueous phase has a first pH, to a second pH, to obtain a remaining aqueous phase and a solid fraction containing an amount of the fusion protein; (2) separating the solid fraction from the remaining aqueous phase, to obtain a separated solid fraction; and (3) dissolving the separated solid fraction in a solution having a pH of 12 or lower but higher than the second pH by at least 0.1 pH units, wherein the protein having a self-assembly capability is a cell surface protein.

The present disclosure provides a method of producing bivalirudin using a peptide fragment or peptide fragments on solid phase peptide synthesis that minimizes, or eliminates, the production of bivalirudin molecules having too few or too many glycine residues.

The present disclosure provides a method of producing bivalirudin using a peptide fragment or peptide fragments on solid phase peptide synthesis that minimizes, or eliminates, the production of bivalirudin molecules having too few or too many glycine residues.