Journal
BULLETIN OF THE CHEMICAL SOCIETY OF JAPAN
Volume 79, Issue 11, Pages 1773-1780Publisher
CHEMICAL SOC JAPAN
DOI: 10.1246/bcsj.79.1773
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An N-S acyl shift reaction of thiol-containing peptides in a trifluoroacetic acid (TFA) solution was confirmed by a combination of C-13 NMR spectroscopy, reversed-phase (RP) HPLC, and MS analyses. A model peptide containing a cysteine residue was transformed into an S-peptide in a TFA solution. The S-peptide was quickly transformed to the original peptide during RP-HPLC analysis even when an eluent that contained 0.1% TFA was used. A peptide that had an N-2-mercapto-4,5-dimethoxybenzyl (Dmmb) group was also transformed into an S-peptide, forming a thioester bond with the thiol of the Dmmb group by TFA treatment. The generated S-peptide was isolated by directly injecting the reaction mixture into a RP-HPLC and was readily converted to the corresponding 2-sulfoethyl thioester via an intermolecular thiol exchange reaction with sodium 2-mercaptoethanesulfonate. The 2-sulfoethyl peptide thioester is widely used as a building block in polypeptide synthesis. The N-S acyl shift reaction observed in peptides with or without an auxiliary group provides a new route for the preparation of peptide thioesters.
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