Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking
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Date
2017-11-28
Open Access Location
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier
Rights
Open Access funded by Biotechnology and Biological Sciences Research Council nder a Creative Commons license
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.
Description
Keywords
Collagen, Molecular dynamics, Ageing, Glycation, Protein cross-linking, Molecular biomechanics
Citation
JOURNAL OF BIOMECHANICS, 2018, 67 pp. 55 - 61