title: The C-Terminal O-S Acyl Shift Pathway under Acidic Condition to Propose Peptide-Thioesters.
abstract: Peptide-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.
authors.affiliation: Division of Bio-Nanochemistry, Wonkwang University, Iksan 570-749, Korea. 123456@wku.ac.kr.
authors.forename: Bo Mi
authors.initials: BM
authors.lastname: Kim
mesh_terms: D004952:Esters / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009842:Oligopeptides / Q000138:chemical synthesis*; D013237:Stereoisomerism; D013438:Sulfhydryl Compounds / Q000138:chemical synthesis*
chemical_list: D004952:Esters; D009842:Oligopeptides; D013438:Sulfhydryl Compounds
keywords: C-terminal handles; acid-catalyzed O-S acyl shift; peptide thioesters