Fibrin mechanical properties and their structural origins.
Fibrin mechanical properties and their structural origins.
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DOI：
10.1016/j.matbio.2016.08.003
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发表时间：
2017-07
期刊：
影响因子：
--
通讯作者：
Weisel JW
中科院分区：
文献类型：
--
作者：
Litvinov RI;Weisel JW
纤维蛋白酶是一种蛋白质聚合物，对于止血和血栓形成、伤口愈合以及涉及细胞外基质的几种其他生物功能和病理状况是必需的。除了分子和细胞的相互作用，纤维蛋白力学最近已被证明是在高度动态的血管内和血管外环境中的凝块行为的基础。纤维素具有弹性和粘性。也许纤维蛋白网络最显著的流变学特征是尽管蛋白质含量非常低，但仍具有极高的弹性和稳定性。另一个重要的机械性能是常见的许多丝状蛋白质聚合物，但不是其他聚合物是硬化发生在响应剪切，张力，或压缩。新的数据已经开始为纤维蛋白的独特力学行为提供结构基础，这种力学行为源于其复杂的多尺度层次结构。整个纤维蛋白凝胶的机械行为主要由单纤维及其集合体的性质决定，包括纤维取向、拉伸、弯曲和屈曲的变化。单个纤维蛋白纤维的性质是由双链半交错原纤维的数量和排列方式决定的，这仍然知之甚少。也有人提出，亚分子结构的强制解折叠，包括纤维蛋白分子的柔性和相对非结构化部分的伸长，可以有助于纤维蛋白变形。尽管我们对纤维蛋白的结构力学的了解有了很大的增加，但关于纤维蛋白的生物学功能的机制仍然是未知的。纤维蛋白可变形性不仅是止血和血栓形成的生物力学的重要组成部分，而且是使用纤维蛋白作为具有特殊和可调节的生物化学和机械性质的多功能生物材料的生物工程的快速发展的领域。
Fibrin is a protein polymer that is essential for hemostasis and thrombosis, wound healing, and several other biological functions and pathological conditions that involve extracellular matrix. In addition to molecular and cellular interactions, fibrin mechanics has been recently shown to underlie clot behavior in the highly dynamic intra- and extravascular environment. Fibrin has both elastic and viscous properties. Perhaps the most remarkable rheological feature of the fibrin network is an extremely high elasticity and stability despite very low protein content. Another important mechanical property that is common to many filamentous protein polymers but not other polymers is stiffening occurring in response to shear, tension, or compression. New data has begun to provide a structural basis for the unique mechanical behavior of fibrin that originates from its complex multi-scale hierarchical structure. The mechanical behavior of the whole fibrin gel is governed largely by the properties of single fibers and their ensembles, including changes in fiber orientation, stretching, bending, and buckling. The properties of individual fibrin fibers are determined by the number and packing arrangements of double-stranded half-staggered protofibrils, which still remain poorly understood. It has also been proposed that forced unfolding of sub-molecular structures, including elongation of flexible and relatively unstructured portions of fibrin molecules, can contribute to fibrin deformations. In spite of a great increase in our knowledge of the structural mechanics of fibrin, much about the mechanisms of fibrin's biological functions remains unknown. Fibrin deformability is not only an essential part of the biomechanics of hemostasis and thrombosis, but also a rapidly developing field of bioengineering that uses fibrin as a versatile biomaterial with exceptional and tunable biochemical and mechanical properties.