Premium
Arginine selective reagents for ligation to peptides and proteins
Author(s) -
Thompson Darren A.,
Ng Raymond,
Dawson Philip E.
Publication year - 2016
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2867
Subject(s) - phenylglyoxal , bioconjugation , chemistry , peptide , combinatorial chemistry , arginine , reagent , covalent bond , protecting group , molecule , peptide synthesis , stereochemistry , biochemistry , amino acid , organic chemistry , alkyl
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.