Collier TANash ABirch HLde Leeuw NH2018-01-232017-11-2228/11/2017JOURNAL OF BIOMECHANICS, 2018, 67 pp. 55 - 610021-9290https://hdl.handle.net/10179/13275Non-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.55 - 61CollagenMolecular dynamicsAgeingGlycationProtein cross-linkingMolecular biomechanicsJournal article10.1016/j.jbiomech.2017.11.0213969351873-2380Massey_Dark0903 Biomedical Engineering0913 Mechanical Engineering1106 Human Movement and Sports Sciences