Combining nano-physical and computational investigations to understand the nature of "aging" in dermal collagen

被引:27
作者
Ahmed, Tarek [1 ]
Nash, Anthony [2 ]
Clark, Kristina E. N. [3 ]
Ghibaudo, Marion [4 ]
de Leeuw, Nora H. [2 ]
Potter, Anne [4 ]
Stratton, Richard [3 ]
Birch, Helen L. [5 ]
Casse, Ramona Enea [4 ]
Bozec, Laurent [1 ]
机构
[1] UCL, Eastman Dent Inst, Div Biomat & Tissue Engn, London, England
[2] UCL, Dept Chem, London, England
[3] UCL, Div Med, Ctr Rheumatol & Connect Tissue Dis, London, England
[4] LOreal Res & Innovat, Aulnay Sous Bois, France
[5] UCL, UCL Inst Orthopaed & Musculoskeletal Sci, Div Surg & Intervent Sci, London, England
基金
英国生物技术与生命科学研究理事会;
关键词
collagen; aging; atomic force microscopy; nanomechanics; advanced glycation end products; nanotechnology; GLYCATION END-PRODUCTS; NORMAL HUMAN-SKIN; LYSYL OXIDASE; CROSS-LINKS; MECHANICAL-PROPERTIES; EXTRACELLULAR-MATRIX; OXIDATIVE STRESS; I COLLAGEN; FIBROBLASTS; EXPRESSION;
D O I
10.2147/IJN.S121400
中图分类号
TB3 [工程材料学];
学科分类号
082905 [生物质能源与材料];
摘要
The extracellular matrix of the dermis is a complex, dynamic system with the various dermal components undergoing individual physiologic changes as we age. Age-related changes in the physical properties of collagen were investigated in particular by measuring the effect of aging, most likely due to the accumulation of advanced glycation end product (AGE) cross-links, on the nanomechanical properties of the collagen fibril using atomic force microscope nano-indentation. An age-related decrease in the Young's modulus of the transverse fibril was observed (from 8.11 to 4.19 GPa in young to old volunteers, respectively, P < 0.001). It is proposed that this is due to a change in the fibril density caused by age-related differences in water retention within the fibrils. The new collagen-water interaction mechanism was verified by electronic structure calculations, showing it to be energetically feasible.
引用
收藏
页码:3303 / 3314
页数:12
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