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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 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: 23 Jan 2018 14:42
URI: http://orca-mwe.cf.ac.uk/id/eprint/107407

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