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首页> 外文期刊>Journal of Biomechanics >THE MECHANICAL PROPERTIES OF SIMULATED COLLAGEN FIBRILS
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THE MECHANICAL PROPERTIES OF SIMULATED COLLAGEN FIBRILS

机译：模拟胶原蛋白原纤的力学性能

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Previous theoretical studies of the mechanical properties of tissues such as skin, bone and tendon, have used approaches based on composite materials and have tended to neglect the contribution of individual microscopic components. In this paper, we examine the relationship between the fine structure of a collagen fibril and its relative tensile strength. Collagen is a fibrous protein which provides associated tissues with the majority of their tensile strength. It is present in the form of elongated structures termed fibrils which are created by the self-assembly of rod-like collagen molecules in an entropy-driven process termed fibrillogenesis. Mutations that alter the primary structure of the collagen molecule, interfere with this assembly process and can lead to the potentially fatal brittle bone disease, osteogenesis imperfecta. Here we investigate the mechanical properties of a range of computer-generated aggregates. The aggregates, created by the diffusion limited aggregation of rods, were subjected to a simple tensile test based on local rules of damage accumulation. In the test, core samples are 'extracted' from the aggregates, and the network of particles involved in the transmission of stress resolved. Increasing stress applied to the core leads to the removal of individual rods from this network; the tensile strength is determined from the Force necessary to form a discontinuous network. Using this approach, we have shown that collagen fibril morphology is critical in determining its tensile strength. We suggest a possible mechanism to account for the increasing severity of osteogenesis imperfecta associated with the distance of mutation from the N-terminal of the collagen molecule. (C) 1997 Elsevier Science Ltd. [References: 16]
机译：先前对组织（如皮肤，骨骼和肌腱）的机械特性进行的理论研究已经使用了基于复合材料的方法，并且往往忽略了各个微观组件的作用。在本文中，我们研究了胶原原纤维的精细结构与其相对抗张强度之间的关系。胶原蛋白是一种纤维蛋白，可为相关组织提供大部分抗张强度。它以被称为原纤维的细长结构的形式存在，该结构是由棒状胶原分子在被称为原纤维形成的熵驱动过程中自组装而成的。改变胶原蛋白分子主要结构的突变会干扰该组装过程，并可能导致潜在的致命脆性骨病，成骨不全症。在这里，我们研究了一系列计算机生成的骨料的机械性能。由棒的扩散受限聚集产生的聚集体，根据局部损伤累积规则进行了简单的拉伸测试。在测试中，将核心样品从聚集体中“提取”出来，并消除了应力传递过程中涉及的颗粒网络。施加到型芯上的应力增加导致从该网络中移除单个杆;拉伸强度由形成不连续网络所需的力决定。使用这种方法，我们已经表明，胶原纤维的形态对确定其拉伸强度至关重要。我们建议一种可能的机制来解释成骨不全症的严重程度与胶原分子N端的突变距离有关。 （C）1997 Elsevier Science Ltd. [引用：16]

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