Reagentless Oxidative Folding of Disulfide‐Rich Peptides Catalyzed by an Intramolecular Diselenide

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Abstract
Building bridges: In cysteine‐rich peptides, diselenides can be used as a proxy for disulfide bridges as the energetic preference for SeSe bonds over mixed SeS 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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