期刊
JOURNAL OF PEPTIDE SCIENCE
卷 17, 期 1, 页码 1-7出版社
WILEY
DOI: 10.1002/psc.1283
关键词
oxidative folding; disulfide; ClearOx; glutathione; diselenide; conotoxin; protocol; selenocysteine; cysteine-rich peptides
资金
- N.I.H. [GM 48677]
- Willard Eccles Fellowship
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM048677] Funding Source: NIH RePORTER
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.
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