Abstract
We tested two alternative oxidation strategies to produce conotoxins α-GI and μ-PIIIA. The peptides were either reversibly immobilized on a solid support and then oxidized, or the immobilized disulfide reagent (CLEAR-OX™) was used to oxidize the peptides. Both strategies appeared more efficient at higher peptide concentrations, consistent with pseudo-dilution effects.
Keywords: Conotoxins, Oxidative folding, Immobilized, CLEAR-OXTM
Protein & Peptide Letters
Title: Oxidative Folding of Conotoxins in Immobilized Systems
Volume: 13 Issue: 1
Author(s): B. R. Green and G. Bulaj
Affiliation:
Keywords: Conotoxins, Oxidative folding, Immobilized, CLEAR-OXTM
Abstract: We tested two alternative oxidation strategies to produce conotoxins α-GI and μ-PIIIA. The peptides were either reversibly immobilized on a solid support and then oxidized, or the immobilized disulfide reagent (CLEAR-OX™) was used to oxidize the peptides. Both strategies appeared more efficient at higher peptide concentrations, consistent with pseudo-dilution effects.
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Cite this article as:
Green R. B. and Bulaj G., Oxidative Folding of Conotoxins in Immobilized Systems, Protein & Peptide Letters 2006; 13 (1) . https://dx.doi.org/10.2174/092986606774502162
DOI https://dx.doi.org/10.2174/092986606774502162 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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