Improved deprotection in solid phase peptide synthesis: quantitative reduction of methionine sulfoxide to methionine during HF cleavage

The reduction of methionine sulfoxide residues in peptides was found to be quantitative by treatment with a low concentration of HF in dimethylsulfide (HF:dimethylsulfide, 1:3, v/v). The reduction was dependent on the acidity function of HF and was optimal with an HF concentration between 25% and 40%. The low HF concentration cleavage reagent also deprotected most of the benzyl alcohol-derived protecting groups.