Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking

Collier, T.A., Nash, A., Birch, H.L. and De Leeuw, Nora ORCID: https://orcid.org/0000-0002-8271-0545 2018. Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking. Journal of Biomechanics 67 , pp. 55-61. 10.1016/j.jbiomech.2017.11.021

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Abstract

Non-enzymatic advanced glycation end product (AGE) cross-linking of collagen molecules has been hypothesised to result in significant changes to the mechanical properties of the connective tissues within the body, potentially resulting in a number of age related diseases. We have investigated the effect of two of these cross-links, glucosepane and DOGDIC, on the tensile and lateral moduli of the collagen molecule through the use of a steered molecular dynamics approach, using previously identified preferential formation sites for intra-molecular cross-links. Our results show that the presence of intra-molecular AGE cross-links increases the tensile and lateral Young’s moduli in the low strain domain by between 3.0 - 8.5 % and 2.9 - 60.3 % respectively, with little effect exhibited at higher strains.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Cardiff Catalysis Institute (CCI) Chemistry
Publisher:	Elsevier
ISSN:	0021-9290
Funders:	BBSRC and EPSRC
Date of First Compliant Deposit:	7 December 2017
Date of Acceptance:	23 November 2017
Last Modified:	04 May 2023 21:55
URI:	https://orca.cardiff.ac.uk/id/eprint/107407

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