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Disulfide bonds of peptides were effectively established between S-protected cysteine residues as well as free cysteine residues by the action of dimethylsulfoxide in trifluoroacetic acid. Oxytocin and alpha-human calcitonin gene-related peptide were synthesized using this oxidation system. The feasibility of this method for the formation of two disulfide bridges of apamin was also examined.

Investigation of the Dimethylsulfoxide-Trifluoroacetic Acid Oxidation System for the Synthesis of Cystine-Containing Peptides.