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

T.A Collier,A Nash,H.L Birch,N.H De Leeuw

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.

Highlights

Collagen is one of the major contributors to the mechanical properties of mammalian tissues
Type I collagen provides the tensile strength to these connective tissues, but it serves as a structural framework for the attachment of cell and other extracellular matrix (ECM) biomolecules (Sweeney et al, 2008)
With collagen making up a significant proportion of connective tissues, approximately 90% in some cases (Kannus, 2000), its biomechanical and energy storage properties are of utmost importance (Franchi et al, 2007)

Summary

Introduction

Collagen is one of the major contributors to the mechanical properties of mammalian tissues. Type I collagen is typically found in connective tissues such as tendon, ligament, bone, skin and the cornea of the eyes of vertebrates (Bhattacharjee and Bansal, 2005). Type I collagen provides the tensile strength to these connective tissues, but it serves as a structural framework for the attachment of cell and other extracellular matrix (ECM) biomolecules (Sweeney et al, 2008). With collagen making up a significant proportion of connective tissues, approximately 90% in some cases (Kannus, 2000), its biomechanical and energy storage properties are of utmost importance (Franchi et al, 2007). The mechanical functions of the supramolecular structure in collagenous tissues are optimised for the direction and magnitude of load. Tendons have unidirectional tensile strength, a consequence of fibre alignment in thick bundles parallel to the long axis of the tendon

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