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Expanding the scope of N → S acyl transfer in native peptide sequences.
Cowper, Ben; Shariff, Leila; Chen, Wenjie; Gibson, Samantha M; Di, Wei-Li; Macmillan, Derek.
Afiliação
  • Cowper B; Department of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK. d.macmillan@ucl.ac.uk.
Org Biomol Chem ; 13(27): 7469-76, 2015 Jul 21.
Article em En | MEDLINE | ID: mdl-26066020
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).
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos / Enxofre / Nitrogênio Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2015 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Peptídeos / Enxofre / Nitrogênio Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2015 Tipo de documento: Article