Issue 26, 2016
From the journal:

Organic & Biomolecular Chemistry

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

Anne C. Conibear, ORCID logo a   Karine Farbiarz,a   Rupert L. Mayer, ORCID logo bc   Maria Matveenko,a   Hanspeter Kähligd  and  Christian F. W. Becker*a  

* Corresponding authors

a University of Vienna, Faculty of Chemistry, Institute of Biological Chemistry, Währinger Straße 38, 1090 Vienna, Austria
E-mail: christian.becker@univie.ac.at
Fax: +43 1 4277 870510
Tel: +43 1 4277 70510

b University of Vienna, Faculty of Chemistry, Institute of Analytical Chemistry, Währinger Straße 38, 1090 Vienna, Austria

c University of Vienna, Faculty of Chemistry, Mass Spectrometry Centre, Währinger Straße 38, 1090 Vienna, Austria

d University of Vienna, Faculty of Chemistry, Institute of Organic Chemistry, Währinger Straße 38, 1090 Vienna, Austria

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.

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

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Article information

DOI
https://doi.org/10.1039/C6OB00932H
Article type
Communication
Submitted
29 Apr 2016
Accepted
01 Jun 2016
First published
02 Jun 2016

Org. Biomol. Chem., 2016,14, 6205-6211

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

A. C. Conibear, K. Farbiarz, R. L. Mayer, M. Matveenko, H. Kählig and C. F. W. Becker, Org. Biomol. Chem., 2016, 14, 6205 DOI: 10.1039/C6OB00932H

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