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

  • J Biomech. 2018 Jan 23;67:55-61. doi: 10.1016/j.jbiomech.2017.11.021.
T A Collier  1 ,  A Nash  2 ,  H L Birch  3 ,  N H de Leeuw  4
Affiliations
  • 1. Institute of Natural and Mathematical Sciences, Massey University, Auckland 0632, New Zealand.
  • 2. Department of Physiology, Anatomy and Genetics, University of Oxford, South Parks Road, Oxford OX1 3QX, United Kingdom.
  • 3. Institute of Orthopaedics and Musculoskeletal Science, UCL, RNOH Stanmore Campus, London, United Kingdom.
  • 4. School of Chemistry, Cardiff University, Cardiff CF10 1DF, United Kingdom. Electronic address: [email protected].
PMID: 29254633 DOI: 10.1016/j.jbiomech.2017.11.021
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
Ageing; Collagen; Glycation; Molecular biomechanics; Molecular dynamics; Protein cross-linking.
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