Journal
JOURNAL OF PEPTIDE SCIENCE
Volume 22, Issue 5, Pages 311-319Publisher
WILEY
DOI: 10.1002/psc.2867
Keywords
bioconjugation; arginine; triazole; chemical ligation
Funding
- NIH [GM098871]
- Sigma-Aldrich Corporation
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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 (C) 2016 European Peptide Society and John Wiley & Sons, Ltd.
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