Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/101685
Title: Allenamides as orthogonal handles for selective modification of cysteine in peptides and proteins
Authors: Abbas, Ata
Xing, Bengang
Loh, Teck-Peng
Keywords: DRNTU::Science::Chemistry
Issue Date: 2014
Source: Abbas, A., Xing, B., & Loh, T.-P. (2014). Allenamides as Orthogonal Handles for Selective Modification of Cysteine in Peptides and Proteins. Angewandte Chemie International Edition, 53(29), 7491-7494.
Series/Report no.: Angewandte chemie international edition
Abstract: In this study, a remarkably simple and direct strategy has been successfully developed to selectively label target cysteine residues in fully unprotected peptides and proteins. The strategy is based on the reaction between allenamides and the cysteine thiol, and proceeds swiftly in aqueous medium with excellent selectivity and quantitative conversion, thus forming a stable and irreversible conjugate. The combined simplicity and mildness of the process project allenamide as robust and versatile handles to target cysteines and has potential use in biological systems. Additionally, fluorescent-labeling studies demonstrated that the installation of a C-terminal allenamide moiety onto various molecules of interest may supply a new methodology towards the site-specific labeling of cysteine-containing proteins. Such a new labeling strategy may thus open a window for its application in the field of life sciences.
URI: https://hdl.handle.net/10356/101685
http://hdl.handle.net/10220/19758
ISSN: 1433-7851
DOI: 10.1002/anie.201403121
Rights: © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SPMS Journal Articles

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