We thank Professors David Blair, David Goldenberg, and Donald Hilvert for helpful discussions and comments on the manuscript. We also acknowledge the assistance of the Peptide Synthesis and Mass Spectrometry Core Facilities at the University of Utah. This work was supported by the NIH Program Project Grant GM 48677.
Reagentless Oxidative Folding of Disulfide-Rich Peptides Catalyzed by an Intramolecular Diselenide†
Article first published online: 27 MAR 2012
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 51, Issue 23, pages 5580–5584, June 4, 2012
How to Cite
Steiner, A. M., Woycechowsky, K. J., Olivera, B. M. and Bulaj, G. (2012), Reagentless Oxidative Folding of Disulfide-Rich Peptides Catalyzed by an Intramolecular Diselenide. Angew. Chem. Int. Ed., 51: 5580–5584. doi: 10.1002/anie.201200062
- Issue published online: 30 MAY 2012
- Article first published online: 27 MAR 2012
- Manuscript Revised: 3 MAR 2012
- Manuscript Received: 4 JAN 2012
- NIH. Grant Number: GM 48677
- protein folding;
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.