Chemoselective peptide bond formation using formyl-substituted nitrophenylthio ester

A novel method for peptide bond formation utilizing amino acid 2-formyl-4-nitrophenylthio ester has been developed. The reaction can be performed in water-containing media and is compatible with various types of amino acid side-chain functional groups. Use of N-methylmaleinimide as an additive is es...

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Bibliographic Details
Published inTetrahedron letters Vol. 44; no. 15; pp. 3187 - 3190
Main Authors Ishiwata, A, Ichiyanagi, T, Takatani, M, Ito, Y
Format Journal Article
LanguageEnglish
Published OXFORD Elsevier 07.04.2003
Subjects
Chemistry
Chemistry, Organic
Physical Sciences
Science & Technology
OLIGOSACCHARIDES
STAUDINGER LIGATION
CHEMICAL LIGATION
RESIDUE
THIOESTER
PROTEINS
AZIDE
AUXILIARY
CYSTEINE-CONTAINING POLYPEPTIDE
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Summary:A novel method for peptide bond formation utilizing amino acid 2-formyl-4-nitrophenylthio ester has been developed. The reaction can be performed in water-containing media and is compatible with various types of amino acid side-chain functional groups. Use of N-methylmaleinimide as an additive is essential for the reaction to proceed with high efficiency. It captures liberated formyl-substituted thiophenol through 1,4-addition followed by aldol cyclization. (C) 2003 Elsevier Science Ltd. All rights reserved.
ISSN:0040-4039
DOI:10.1016/S0040-4039(03)00471-4