Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 17, Issue 1, Pages 1-7Publisher
WILEY
DOI: 10.1002/psc.1283
Keywords
oxidative folding; disulfide; ClearOx; glutathione; diselenide; conotoxin; protocol; selenocysteine; cysteine-rich peptides
Funding
- N.I.H. [GM 48677]
- Willard Eccles Fellowship
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM048677] Funding Source: NIH RePORTER
Ask authors/readers for more resources
The oxidative folding of small, cysteine-rich peptides to selectively achieve the native disulfide bond connectivities is critical for discovery and structure-function studies of many bioactive peptides. As the propensity to acquire the native conformation greatly depends on the peptide sequence, numerous empirical oxidation methods are employed. The context-dependent optimization of these methods has thus far precluded a generalized oxidative folding protocol, in particular for peptides containing more than two disulfides. Herein, we compare the efficacy of optimized solution-phase and polymer-supported oxidation methods using three disulfide-bridged conotoxins, namely mu-SIIIA, mu-KIIIA and omega-GVIA. The use of diselenide bridges as proxies for disulfide bridges is also evaluated. We propose the ClearOx-assisted oxidation of selenopeptides as a fairly generalized oxidative folding protocol. Copyright (C) 2010 European Peptide Society and John Wiley & Sons, Ltd.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available