Issue 27, 2015

Expanding the scope of N → S acyl transfer in native peptide sequences

Abstract

Understanding the factors that influence N → S acyl transfer in native peptide sequences, and discovery of new reagents that facilitate it, will be key to expanding its scope and applicability. Here, through a study of short model peptides in thioester formation and cyclisation reactions, we demonstrate that a wider variety of Xaa-Cys motifs than originally envisaged are capable of undergoing efficient N → S acyl transfer. We present data for the relative rates of thioester formation and cyclisation for a representative set of amino acids, and show how this expanded scope can be applied to the production of the natural protease inhibitor Sunflower Trypsin Inhibitor-1 (SFTI-1).

Graphical abstract: Expanding the scope of N → S acyl transfer in native peptide sequences

Supplementary files

Article information

Article type
Paper
Submitted
21 May 2015
Accepted
04 Jun 2015
First published
04 Jun 2015

Org. Biomol. Chem., 2015,13, 7469-7476

Author version available

Expanding the scope of N → S acyl transfer in native peptide sequences

B. Cowper, L. Shariff, W. Chen, S. M. Gibson, W. Di and D. Macmillan, Org. Biomol. Chem., 2015, 13, 7469 DOI: 10.1039/C5OB01029B

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