title: Oxidative folding of conotoxins in immobilized systems.
abstract: We tested two alternative oxidation strategies to produce conotoxins alpha-GI and micro-PIIIA. The peptides were either reversibly immobilized on a solid support and then oxidized, or the immobilized disulfide reagent (CLEAR-OX(trade mark)) was used to oxidize the peptides. Both strategies appeared more efficient at higher peptide concentrations, consistent with pseudo-dilution effects.
authors.affiliation: Cognetix, Inc., 421 Wakara Way, Suite 201, Salt Lake City, Utah 84108, USA.
authors.forename: Brad R
authors.initials: BR
authors.lastname: Green
authors.forename: Grzegorz
authors.initials: G
authors.lastname: Bulaj
mesh_terms: D000595:Amino Acid Sequence; D020916:Conotoxins / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D017510:Protein Folding
chemical_list: D020916:Conotoxins; D004220:Disulfides