Arginine side-chain modification that occurs during copper-catalysed azide-alkyne click reactions resembles an advanced glycation end product

Anne C Conibear; Karine Farbiarz; Rupert L Mayer; Maria Matveenko; Hanspeter Kählig; Christian F W Becker

doi:10.1039/c6ob00932h

Arginine side-chain modification that occurs during copper-catalysed azide-alkyne click reactions resembles an advanced glycation end product

Org Biomol Chem. 2016 Jul 14;14(26):6205-11. doi: 10.1039/c6ob00932h. Epub 2016 Jun 10.

Authors

Anne C Conibear¹, Karine Farbiarz, Rupert L Mayer, Maria Matveenko, Hanspeter Kählig, Christian F W Becker

Affiliation

¹ University of Vienna, Faculty of Chemistry, Institute of Biological Chemistry, Währinger Straße 38, 1090 Vienna, Austria. christian.becker@univie.ac.at.

PMID: 27282129
DOI: 10.1039/c6ob00932h

Abstract

Dehydroascorbate is a by-product of copper-catalysed azide-alkyne click (CuAAC) reactions and also forms advanced glycation end products (AGEs) in tissues undergoing oxidative stress. Here we isolate and characterize an arginine-dehydroascorbate adduct formed during CuAAC reactions, investigate strategies for preventing its formation, and propose its biological relevance as an AGE.

MeSH terms

Alkynes / chemistry*
Arginine / chemistry*
Azides / chemistry*
Catalysis
Click Chemistry
Copper / chemistry*
Dehydroascorbic Acid / chemical synthesis*
Dehydroascorbic Acid / chemistry
Glycation End Products, Advanced / chemical synthesis*
Glycation End Products, Advanced / chemistry
Molecular Structure

Substances

Alkynes
Azides
Glycation End Products, Advanced
Copper
Arginine
Dehydroascorbic Acid