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Molecules 2016, 21(11), 1559; doi:10.3390/molecules21111559

The C-Terminal O-S Acyl Shift Pathway under Acidic Condition to Propose Peptide-Thioesters

Division of Bio-Nanochemistry, Wonkwang University, Iksan 570-749, Korea
Academic Editor: Roman Dembinski
Received: 21 September 2016 / Revised: 3 November 2016 / Accepted: 11 November 2016 / Published: 17 November 2016
(This article belongs to the Section Organic Synthesis)
View Full-Text   |   Download PDF [1375 KB, uploaded 17 November 2016]   |  

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. View Full-Text
Keywords: C-terminal handles; peptide thioesters; acid-catalyzed O-S acyl shift C-terminal handles; peptide thioesters; acid-catalyzed O-S acyl shift
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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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.

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