In situ thioester formation for protein ligation using α-methylcysteine

Fabienne Burlina; George Papageorgiou; Caroline Morris; Peter D. White; John Offer

doi:10.1039/c3sc52140k

In situ thioester formation for protein ligation using α-methylcysteine

Fabienne Burlina, George Papageorgiou, Caroline Morris, Peter D. White, John Offer^*

^*Corresponding author for this work

School of Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The progress of total chemical protein synthesis has been hampered by difficulties in preparing peptide thioesters by standard Fmoc peptide synthesis. The amino acid, α-methylcysteine, sited at the C-terminus of a peptide can substitute for a thioester in peptide ligation reactions. C-terminal α-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.

Original language	English
Pages (from-to)	766-770
Number of pages	5
Journal	Chemical Science
Volume	5
Issue number	2
Early online date	20 Nov 2013
DOIs	https://doi.org/10.1039/c3sc52140k
Publication status	E-pub ahead of print - 20 Nov 2013

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title = "In situ thioester formation for protein ligation using α-methylcysteine",

abstract = "The progress of total chemical protein synthesis has been hampered by difficulties in preparing peptide thioesters by standard Fmoc peptide synthesis. The amino acid, α-methylcysteine, sited at the C-terminus of a peptide can substitute for a thioester in peptide ligation reactions. C-terminal α-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.",

author = "Fabienne Burlina and George Papageorgiou and Caroline Morris and White, \{Peter D.\} and John Offer",

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T1 - In situ thioester formation for protein ligation using α-methylcysteine

AU - Burlina, Fabienne

AU - Papageorgiou, George

AU - Morris, Caroline

AU - White, Peter D.

AU - Offer, John

PY - 2013/11/20

Y1 - 2013/11/20

N2 - The progress of total chemical protein synthesis has been hampered by difficulties in preparing peptide thioesters by standard Fmoc peptide synthesis. The amino acid, α-methylcysteine, sited at the C-terminus of a peptide can substitute for a thioester in peptide ligation reactions. C-terminal α-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.

AB - The progress of total chemical protein synthesis has been hampered by difficulties in preparing peptide thioesters by standard Fmoc peptide synthesis. The amino acid, α-methylcysteine, sited at the C-terminus of a peptide can substitute for a thioester in peptide ligation reactions. C-terminal α-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.

U2 - 10.1039/c3sc52140k

DO - 10.1039/c3sc52140k

M3 - Article

AN - SCOPUS:84891388712

SN - 2041-6520

VL - 5

SP - 766

EP - 770

JO - Chemical Science

JF - Chemical Science

IS - 2

ER -

In situ thioester formation for protein ligation using α-methylcysteine

Abstract

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