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Article Dans Une Revue Chemical Science Année : 2013

In situ thioester formation for protein ligation using a-methylcysteine

Résumé

The progress of total chemical protein synthesis has been hampered by difficulties in preparing peptide thioesters by standard Fmoc peptide synthesis. The amino acid, a-methylcysteine, sited at the C-terminus of a peptide can substitute for a thioester in peptide ligation reactions. C-terminal a-methylcysteine is fully compatible with Fmoc peptide synthesis and its use in ligation is very simple and robust. Its potential is demonstrated with the synthesis of model proteins.

Domaines

Chimie
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Dates et versions

hal-01118189 , version 1 (18-02-2015)

Identifiants

Citer

Fabienne Burlina, George Papageorgiou, Caroline Morris, Peter D. White, John Offer. In situ thioester formation for protein ligation using a-methylcysteine. Chemical Science, 2013, 5 (2), pp.766-770. ⟨10.1039/c3sc52140k⟩. ⟨hal-01118189⟩
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