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Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation.

ABSTRACT: Selective protein cleavage at methionine residues is a useful method for the production of bacterially derived protein fragments containing an N-terminal cysteine residue required for native chemical ligation. Here we describe an optimised procedure for cyanogen bromide-mediated protein cleavage, and ligation of the resulting fragments to afford biologically active proteins.

SUBMITTER: Richardson JP

PROVIDER: S-EPMC2898651 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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Optimisation of chemical protein cleavage for erythropoietin semi-synthesis using native chemical ligation.

Richardson Jonathan P JP Macmillan Derek D

Organic & biomolecular chemistry 20080905 21

Selective protein cleavage at methionine residues is a useful method for the production of bacterially derived protein fragments containing an N-terminal cysteine residue required for native chemical ligation. Here we describe an optimised procedure for cyanogen bromide-mediated protein cleavage, and ligation of the resulting fragments to afford biologically active proteins. ...[more]

PMID: 18931805

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