Disulfide bond formation in S‐acetamidomethyl (Acm) cysteine‐containing peptides by successive treatments with silver trifluoromethanesulfonate (AgOTf) and dimethyl sulfoxide (DMSO)/aqueous HCl is described. An S‐Acm cysteine was found to be quantitatively converted into cystine by deprotection of the Acm group with AgOTf followed by DMSO/aqueous HCl treatment. Under these reaction conditions, no significant side reactions were observed with oxidation‐sensitive amino acids such as Met, Tyr and Trp. Oxytocin and a Trp‐containing peptide, urotensin II, were prepared by this method. Furthermore, regioselective two disulfide bond formation was found to be feasible by the combination of air oxidation and the AgOTf‐DMSO/HCl system. This strategy has been successfully applied to the syntheses of tachyplesin I and endothelin I, which have two disulfide bonds and a Trp residue in the molecule.
|ジャーナル||International Journal of Peptide and Protein Research|
|出版ステータス||Published - 1995 4月|
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