Elsevier

Journal of Biomechanics

Volume 67, 23 January 2018, Pages 55-61
Journal of Biomechanics

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

https://doi.org/10.1016/j.jbiomech.2017.11.021Get rights and content
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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.

Keywords

Collagen
Molecular dynamics
Ageing
Glycation
Protein cross-linking
Molecular biomechanics

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