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Chemoselective peptide bond formation using formyl-substituted nitrophenylthio ester

✍ Scribed by Akihiro Ishiwata; Tsuyoshi Ichiyanagi; Maki Takatani; Yukishige Ito

Book ID: 104253335
Publisher: Elsevier Science
Year: 2003
Tongue: French
Weight: 242 KB
Volume: 44
Category: Article
ISSN: 0040-4039
DOI: 10.1016/s0040-4039(03)00471-4

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✦ Synopsis

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.

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✍ V. V. Kotusov; M. K. Kukhanova; A. A. Krayevsky; B. P. Gottikh 📂 Article 📅 1976 🏛 Springer 🌐 English ⚖ 275 KB

50 S subunits of E. coli ribosomes catalyze the reaction of the 2'(3')-N-(formyl) methionine ester of adenosine 5'-phosphate and Phe-tRNA resulting in peptide bond synthesis. Cytidine 5'-phosphate stimulates this process on 50 S ribosomal subunits as well as on intact ribosomes. The obtained data sh