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Hydrogen peroxide for disulfide bridge formation in methionine‐containing peptides 1
Author(s) -
Kudryavtseva Elena V.,
Sidorova Mariya V.,
Ovchinnikov Mikhail V.,
Bespalova Zhanna D.
Publication year - 2000
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/(sici)1099-1387(200005)6:5<208::aid-psc241>3.0.co;2-v
Subject(s) - hydrogen peroxide , chemistry , disulfide bond , methionine , hydrogen bond , sulfoxide , regioselectivity , combinatorial chemistry , stereochemistry , biochemistry , amino acid , organic chemistry , molecule , catalysis
Two methionine‐containing peptides, endothelin 1 and the 1–16 fragment of the receptor of the plasminogen activator 1 for human urokinase, were synthesized and cyclized by hydrogen peroxide. Endothelin 1 was obtained by using regioselective and random schemes of disulfide bond formation. The conditions of cyclization that provided the target products in high purity were found. The general potential of disulfide bond formation by means of hydrogen peroxide was demonstrated for methionine‐containing peptides. The method resulted in target products containing insignificant quantities of the corresponding Met‐sulfoxide derivatives. Copyright © 2000 European Peptide Society and John Wiley & Sons, Ltd.