Premium
Isopeptide method: development of S ‐acyl isopeptide method for the synthesis of difficult sequence‐containing peptides
Author(s) -
Yoshiya Taku,
Ito Nui,
Kimura Tooru,
Kiso Yoshiaki
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1053
Subject(s) - pentapeptide repeat , chemistry , peptide , sequence (biology) , acylation , combinatorial chemistry , peptide synthesis , intramolecular force , nucleophilic acyl substitution , stereochemistry , biochemistry , catalysis
A novel strategy for a more efficient synthesis of difficult sequence‐containing peptides, the S ‐acyl isopeptide method, was developed and successfully applied. A model pentapeptide Ac–Val–Val–Cys–Val–Val–NH 2 was synthesized via its water‐soluble S ‐acyl isopeptide using an S ‐acyl isodipeptide unit, Boc–Cys(Fmoc–Val)–OH. An S ‐acyl isopeptide possessing excellent water solubility could be readily and quantitatively converted to the native peptide via an S N intramolecular acyl migration reaction at pH 7.4. Thus, the S ‐acyl isopeptide method provides a useful tool in peptide chemistry. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.