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Reagentless Oxidative Folding of Disulfide‐Rich Peptides Catalyzed by an Intramolecular Diselenide
Author(s) -
Steiner Andrew M.,
Woycechowsky Kenneth J.,
Olivera Baldomero M.,
Bulaj Grzegorz
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201200062
Subject(s) - oxidative folding , diselenide , intramolecular force , disulfide bond , cysteine , chemistry , folding (dsp implementation) , bridging (networking) , catalysis , oxidative phosphorylation , protein disulfide isomerase , protein folding , combinatorial chemistry , stereochemistry , organic chemistry , biochemistry , selenium , computer science , electrical engineering , enzyme , engineering , computer network
Building bridges : In cysteine‐rich peptides, diselenides can be used as a proxy for disulfide bridges as the energetic preference for SeSe bonds over mixed SeS bonds simplifies folding (see picture). An intramolecular diselenide bond efficiently catalyzes the oxidative folding of selenopeptide analogues of conotoxins, and serves as a reagentless method to accelerate formation of various native disulfide bridging patterns.