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- W1888059172 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)." @default.
- W1888059172 created "2016-06-24" @default.
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- W1888059172 date "2015-01-01" @default.
- W1888059172 modified "2023-10-09" @default.
- W1888059172 title "Expanding the scope of N → S acyl transfer in native peptide sequences" @default.
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- W1888059172 doi "https://doi.org/10.1039/c5ob01029b" @default.
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