Department of Biomedical Engineering, Southern University of Science and Technology, Shenzhen 518055, P. R. China.
Department of Physics and Key Laboratory of Artificial Micro- and Nano-structures of Ministry of Education, School of Physics and Technology, Wuhan University, Wuhan 430072, P. R. China.
Sci Rep. 2017 Apr 5;7:46042. doi: 10.1038/srep46042.
Collagen, the dominating material in the extracellular matrix, provides the strength, elasticity and mechanical stability to the organisms. The mechanical property of collagen is mainly dominated by its surrounding environments. However, the variation and origin of the mechanics of collagen fibril under different concentrations of calcium ions (χ) remains unknown. By using the atomic force microscopy based nanoindentation, the mechanics and structure of individual type II collagen fibril were first investigated under different χ in this study. The results demonstrate that both of the mechanical and structural properties of the collagen fibril show a prominent dependence on χ. The mechanism of χ-dependence of the collagen fibril was attributed to the chelation between collagen molecules and the calcium ions. Given the role of calcium in the pathology of osteoarthritis, the current study may cast new light on the understanding of osteoarthritis and other soft tissue hardening related diseases in the future.
胶原蛋白是细胞外基质中的主要物质,为生物体提供强度、弹性和机械稳定性。胶原蛋白的力学性能主要由其周围环境决定。然而,在不同浓度钙离子(χ)下胶原原纤维力学性质的变化和起源尚不清楚。本研究首次通过原子力显微镜纳米压痕法研究了不同 χ 下单个 II 型胶原原纤维的力学和结构。结果表明,胶原原纤维的力学和结构性能都明显依赖于 χ。胶原原纤维对 χ 的依赖性机制归因于胶原蛋白分子与钙离子的螯合作用。鉴于钙在骨关节炎发病机制中的作用,本研究可能为未来理解骨关节炎和其他与软组织硬化相关的疾病提供新的思路。