Expanding the scope of N â S acyl transfer in native peptide sequences.
Org Biomol Chem
; 13(27): 7469-76, 2015 Jul 21.
Article
em En
| MEDLINE
| ID: mdl-26066020
ABSTRACT
Understanding the factors that influence N â 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 â 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).
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