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Issue 27, 2015
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Expanding the scope of N → S acyl transfer in native peptide sequences

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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

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Publication details

The article was received on 21 May 2015, accepted on 04 Jun 2015 and first published on 04 Jun 2015


Article type: Paper
DOI: 10.1039/C5OB01029B
Author version available: Download Author version (PDF)
Citation: Org. Biomol. Chem., 2015,13, 7469-7476
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    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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