Abstract
Oxidative disulfide bond formations have been applied to soluble-tag-assisted method successfully to realize the total synthesis of α-conotoxin MII (4) that comprises 16 amino acid residues and possesses 2 disulfide bonds. Orthogonal peptide folding using DEAD and iodine oxidations in combination with Mmt and Acm groups for the side chain protection of cysteines could be carried out with no peptide aggregation.
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