Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties
Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties
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DOI：
10.1016/s0006-3495(97)78247-x
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发表时间：
1997-10-01
影响因子：
3.4
通讯作者：
Silver, FH
中科院分区：
文献类型：
--
作者：
Pins, GD;Christiansen, DL;Silver, FH
胶原蛋白是细胞外基质的主要结构元素。它以纤维的形式传递力、耗散能量并防止正常组织过早发生机械故障。胶原纤维的变形涉及分子拉伸和滑移、原纤维滑移，以及最终的除颤。我们的实验室开发了一种宏观胶原纤维自组装工艺，其结构和机械性能与鼠尾腱纤维相似。本研究的目的是确定亚纤维取向和核心蛋白聚糖掺入对胶原纤维机械性能的影响。自组装胶原纤维在交联前拉伸 0-50%，然后通过显微镜和机械测试进行表征。这些研究的结果表明，原纤维取向、堆积和极限拉伸强度可以通过拉伸来增加。此外，研究表明，核心蛋白聚糖的掺入可提高未交联纤维的极限拉伸强度。基于观察到的结果，假设核心蛋白聚糖在变形过程中促进原纤维滑移，从而提高胶原纤维的拉伸性能。
Collagen is the primary structural element in extracellular matrices. In the form of fibers it acts to transmit forces, dissipate energy, and prevent premature mechanical failure in normal tissues. Deformation of collagen fibers involves molecular stretching and slippage, fibrillar slippage, and, ultimately, defibrillation. Our laboratory has developed a process for self-assembly of macroscopic collagen fibers that have structures and mechanical properties similar to rat tail tendon fibers. The purpose of this study is to determine the effects of subfibrillar orientation and decorin incorporation on the mechanical properties of collagen fibers. Self-assembled collagen fibers were stretched 0-50% before cross-linking and then characterized by microscopy and mechanical testing. Results of these studies indicate that fibrillar orientation, packing, and ultimate tensile strength can be increased by stretching. In addition, it is shown that decorin incorporation increases ultimate tensile strength of uncross-linked fibers. Based on the observed results it is hypothesized that decorin facilitates fibrillar slippage during deformation and thereby improves the tensile properties of collagen fibers.