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Oxidative Folding of Conotoxins in Immobilized Systems

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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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Keywords: CLEAR-OXTM; Conotoxins; Immobilized; Oxidative folding

Document Type: Research Article

Affiliations: Cognetix, Inc., 421 Wakara Way, Suite 201, Salt Lake City, Utah 84108, USA.

Publication date: January 1, 2006

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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