Arginine selective reagents for ligation to peptides and proteins. (22nd March 2016)

• Record Type: Journal Article
• Authors: Thompson, Darren A.; Ng, Raymond; Dawson, Philip E.
• Is Part Of: Journal of peptide science. Volume 22:Number 5(2016:May)
• Page Start: 311
• Page End: 319
• Publication Date: 2016-03-22
• Subjects: bioconjugation -- arginine -- triazole -- chemical ligation; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2867
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : A new class of arginine‐specific bioconjugation reagents for protein labeling has been developed. This method utilizes a triazolyl‐phenylglyoxal group on the probe molecule that reacts selectively with the guandinyl group of Arg residues in a protein or peptide. The reaction proceeds in neutral to basic bicarbonate buffers and is selective for arginine residues in peptides and folded proteins. Importantly, the triazolyl‐phenylglyoxal group can be introduced into complex molecules containing alkyne groups using CuAAC chemistry, providing a robust approach for the generation of phenylglyoxal reactive groups into molecules to be covalently attached onto the surface of proteins. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd. Abstract : A new class of arginine‐specific chemoselective bioconjugation reagents for protein labeling has been developed. The phenylglyoxal functional group is introduced by CuAAC reaction facilitating the development of complex labeling reagents.