The C-Terminal O-S Acyl Shift Pathway under Acidic Condition to Propose Peptide-Thioesters
AbstractPeptide-thioester is a pivotal intermediate for peptide ligation and N-, C-terminal cyclization. In this study, desired pathway and the side products of two C-terminal handles, hydroxyethylthiol (HET) and hydroxypropylthiol (HPT) are described in different conditions as well as kinetic studies. In addition, a new mechanism of C-terminal residue racemization is proposed on the basis of differentiation of products derived from the two C-terminal handles in preparing peptide thioesters through an acid-catalyzed tandem thiol switch, first by an intramolecular O-S acyl shift, and then by an intermolecular S-S exchange. View Full-Text
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Kim, B.M. The C-Terminal O-S Acyl Shift Pathway under Acidic Condition to Propose Peptide-Thioesters. Molecules 2016, 21, 1559.
Kim BM. The C-Terminal O-S Acyl Shift Pathway under Acidic Condition to Propose Peptide-Thioesters. Molecules. 2016; 21(11):1559.Chicago/Turabian Style
Kim, Bo M. 2016. "The C-Terminal O-S Acyl Shift Pathway under Acidic Condition to Propose Peptide-Thioesters." Molecules 21, no. 11: 1559.
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