Issue 38, 2014
From the journal:

Chemical Communications

Site-specific cross-linking of collagen peptides by lysyl advanced glycation endproducts†

M. Kamalov,ab   P. W. R. Harris,a   G. J. S. Cooperbcde  and  M. A. Brimble*abc  

* Corresponding authors

a School of Chemical Sciences, The University of Auckland, 23 Symonds Street, Auckland, New Zealand
E-mail: m.brimble@auckland.ac.nz

b Maurice Wilkins Centre for Molecular Biodiscovery, The University of Auckland, 3 Symonds Street, Auckland, New Zealand

c School of Biological Sciences, The University of Auckland, 3 Symonds Street, Auckland, New Zealand

d Centre for Advanced Discovery and Experimental Therapeutics, Central Manchester University Hospitals, NHS Foundation Trust, and the School of Biomedicine, The University of Manchester, Manchester, UK

e Department of Pharmacology, Division of Medical Sciences, University of Oxford, Oxford, UK

Abstract

Cross-linking of proteins by advanced glycation endproducts (AGEs) causes a host of pathological conditions but their exact roles are unknown. Cross-linking lysyl AGEs were synthesized and incorporated into two types of collagen peptides. The utility of these cross-linked peptides for biochemical investigations was demonstrated by proteolysis studies and circular dichroism.

Graphical abstract: Site-specific cross-linking of collagen peptides by lysyl advanced glycation endproducts

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Article information

DOI
https://doi.org/10.1039/C4CC02003K
Article type
Communication
Submitted
17 3 2014
Accepted
27 3 2014
First published
31 3 2014

Chem. Commun., 2014,50, 4944-4946

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Site-specific cross-linking of collagen peptides by lysyl advanced glycation endproducts

M. Kamalov, P. W. R. Harris, G. J. S. Cooper and M. A. Brimble, Chem. Commun., 2014, 50, 4944 DOI: 10.1039/C4CC02003K

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