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: | Research Institutes & Centres > Cardiff Catalysis Institute (CCI) Schools > 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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