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Disulfide bond-forming reaction using a dimethyl sulfoxide/aqueous HCl system and its application to regioselective two disulfide bond formation.

Authors :
Tamamura H
Otaka A
Nakamura J
Okubo K
Koide T
Ikeda K
Ibuka T
Fujii N
Source :
International journal of peptide and protein research [Int J Pept Protein Res] 1995 Apr; Vol. 45 (4), pp. 312-9.
Publication Year :
1995

Abstract

Disulfide bond formation in S-acetamidomethyl (Acm) cysteine-containing peptides by successive treatments with silver trifluoromethanesulfonate (AgOTf) and dimethyl sulfoxide (DMSO)/aqueous HCl is described. An S-Acm cysteine was found to be quantitatively converted into cysteine by deprotection of the Acm group with AgOTf followed by DMSO/aqueous HCl treatment. Under these reaction conditions, no significant side reactions were observed with oxidation-sensitive amino acids such as Met, Tyr and Trp. Oxytocin and a Trp-containing peptide, urotensin II, were prepared by this method. Furthermore, regioselective two disulfide bond formation was found to be feasible by the combination of air oxidation and the AgOTf-DMSO/HCl system. This strategy has been successfully applied to the syntheses of tachyplesin I and endothelin I, which have two disulfide bonds and a Trp residue in the molecule.

Details

Language :
English
ISSN :
0367-8377
Volume :
45
Issue :
4
Database :
MEDLINE
Journal :
International journal of peptide and protein research
Publication Type :
Academic Journal
Accession number :
7601603
Full Text :
https://doi.org/10.1111/j.1399-3011.1995.tb01043.x