Reagentless Oxidative Folding of Disulfide-Rich Peptides Catalyzed by an Intramolecular Diselenide
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 ana...
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Veröffentlicht in: | Angewandte Chemie International Edition 2012-06, Vol.51 (23), p.5580-5584 |
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creator | Steiner, Andrew M. Woycechowsky, Kenneth J. Olivera, Baldomero M. Bulaj, Grzegorz |
description | 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. |
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subjects | Bridges (structures) Bridging Buildings Catalysis Conotoxins - chemistry Conotoxins - metabolism Construction Cysteine - chemistry Disulfides Disulfides - chemistry Folding Formations kinetics oxidation Oxidation-Reduction oxygen Peptides Peptides - chemistry Pictures Protein Folding selenium Selenium - chemistry |
title | Reagentless Oxidative Folding of Disulfide-Rich Peptides Catalyzed by an Intramolecular Diselenide |
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