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

被引：24

作者：

Collier, T. A. ^{[1
]}

Nash, A. ^{[2
]}

Birch, H. L. ^{[3
]}

de Leeuw, N. H. ^{[4
]}

机构：

[1] Massey Univ, Inst Nat & Math Sci, Auckland 0632, New Zealand

[2] Univ Oxford, Dept Physiol Anat & Genet, South Parks Rd, Oxford OX1 3QX, England

[3] UCL, Inst Orthopaed & Musculoskeletal Sci, RNOH Stanmore Campus, London, England

[4] Cardiff Univ, Sch Chem, Cardiff CF10 1DF, S Glam, Wales

来源：

JOURNAL OF BIOMECHANICS | 2018年 / 67卷

基金：

英国生物技术与生命科学研究理事会; 英国工程与自然科学研究理事会;

关键词：

Collagen; Molecular dynamics; Ageing; Glycation; Protein cross-linking; Molecular biomechanics; MOLECULAR-DYNAMICS; ACHILLES-TENDON; NONENZYMATIC GLYCATION; STRUCTURAL HIERARCHY; ELASTIC PROPERTIES; CONNECTIVE-TISSUE; YOUNGS MODULUS; FIBRILS; PROTEIN; MATRIX;

D O I：

10.1016/j.jbiomech.2017.11.021

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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. (C) 2017 The Author(s). Published by Elsevier Ltd.

引用

页码：55 / 61

页数：7

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