title: 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).
authors.affiliation: Department of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK. d.macmillan@ucl.ac.uk.
authors.forename: Ben
authors.initials: B
authors.lastname: Cowper
authors.forename: Leila
authors.initials: L
authors.lastname: Shariff
authors.forename: Wenjie
authors.initials: W
authors.lastname: Chen
authors.forename: Samantha M
authors.initials: SM
authors.lastname: Gibson
authors.forename: Wei-Li
authors.initials: WL
authors.lastname: Di
authors.forename: Derek
authors.initials: D
authors.lastname: Macmillan
mesh_terms: D000215:Acylation; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D066241:Carbon-13 Magnetic Resonance Spectroscopy; D003500:Cyclization; D003545:Cysteine / Q000737:chemistry; D004952:Esters / Q000737:chemistry; D008623:Mercaptoethanol / Q000737:chemistry; D008969:Molecular Sequence Data; D009584:Nitrogen / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry; D066244:Proton Magnetic Resonance Spectroscopy; D013455:Sulfur / Q000737:chemistry*
chemical_list: D004952:Esters; D010455:Peptides; D010456:Peptides, Cyclic; C448501:SFTI-1 peptide, sunflower; D008623:Mercaptoethanol; D013455:Sulfur; D003545:Cysteine; D009584:Nitrogen