Next Article in Journal
Pilot-Scale Production and Thermostability Improvement of the M23 Protease Pseudoalterin from the Deep Sea Bacterium Pseudoalteromonas sp. CF6-2
Previous Article in Journal
A Stereocontrolled Protocol to Highly Functionalized Fluorinated Scaffolds through a Fluoride Opening of Oxiranes
Open AccessArticle

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
Molecules 2016, 21(11), 1559; https://doi.org/10.3390/molecules21111559
Received: 21 September 2016 / Revised: 3 November 2016 / Accepted: 11 November 2016 / Published: 17 November 2016
(This article belongs to the Section Organic Chemistry)
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
Show Figures

Graphical abstract

MDPI and ACS Style

Kim, B.M. The C-Terminal O-S Acyl Shift Pathway under Acidic Condition to Propose Peptide-Thioesters. Molecules 2016, 21, 1559.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map

1
Back to TopTop