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Type: Journal article
Title: Expressed Protein Selenoester Ligation
Author: Kulkarni, S.S.
Watson, E.E.
Maxwell, J.W.C.
Niederacher, G.
Johansen‐Leete, J.
Huhmann, S.
Mukherjee, S.
Norman, A.R.
Kriegesmann, J.
Becker, C.F.W.
Payne, R.J.
Citation: Angewandte Chemie International Edition, 2022; 61(20):e202200163-1-e202200163-6
Publisher: Wiley
Issue Date: 2022
ISSN: 1433-7851
Statement of
Sameer S. Kulkarni, Emma E. Watson, Joshua W. C. Maxwell, Gerhard Niederacher, Jason Johansen-Leete, Susanne Huhmann, Somnath Mukherjee, Alexander R. Norman, Julia Kriegesmann, Christian F. W. Becker, and Richard J. Payne
Abstract: Herein, we describe the development and application of a novel expressed protein selenoester ligation (EPSL) methodology for the one-pot semi-synthesis of modified proteins. EPSL harnesses the rapid kinetics of ligation reactions between modified synthetic selenopeptides and protein aryl selenoesters (generated from expressed intein fusion precursors) followed by in situ chemoselective deselenization to afford target proteins at concentrations that preclude the use of traditional ligation methods. The utility of the EPSL technology is showcased through the efficient semi-synthesis of ubiquitinated polypeptides, lipidated analogues of the membrane-associated GTPase YPT6, and site-specifically phosphorylated variants of the oligomeric chaperone protein Hsp27 at high dilution.
Keywords: Expressed Protein Selenoesters; Peptides; Protein Modifications; Protein Semi-Synthesis; Proteins
Rights: © 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCHGmbH. This is an open access article under the terms of the Creative Commons Attribution License,which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
DOI: 10.1002/anie.202200163
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Appears in Collections:Chemistry publications

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