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Small-angle light scattering to detect strain-directed collagen degradation in native tissue

机译:小角度光散射可检测天然组织中应变导向的胶原蛋白降解

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摘要

It has been demonstrated that there is a mechanochemical relationship between collagen and collagenolytic enzymes such that increased tensile mechanical strain reduces the enzymatic cutting rate. This mechanochemical relationship has the potential to permit directed remodelling of tissue-engineered constructs in vitro and to shed light on the generation of load-adapted collagen-based connective tissue. In this investigation, we demonstrate that small-angle light scattering (SALS) has the sensitivity to dynamically detect the preferential enzymatic degradation of a subset of unloaded collagen fibrils within differentially loaded native tissue. Detection of the difference in the relative degradation rate of unloaded fibrils versus loaded fibrils was manifested through changes in the spatial distribution of the SALS signal. Specifically, we found a linear increase in the eccentricity of the SALS data that was consistent with preferential retention of the collagen fibrils aligned with the applied tensile strain. We conclude that SALS is simple, inexpensive and may provide a useful optical screening method permitting real-time monitoring of strain-controlled tissue and construct remodelling.
机译:已经证明,胶原蛋白和胶原蛋白分解酶之间存在机械化学关系,使得增加的拉伸机械应变降低了酶促切割速率。这种机械化学关系有可能允许在体外对组织工程化的构建体进行直接重塑,并阐明基于负载的胶原基结缔组织的产生。在这项研究中,我们证明了小角度光散射(SALS)具有动态检测在差异加载的天然组织中未加载的胶原原纤维子集的优先酶促降解的灵敏度。通过SALS信号的空间分布的变化,可以检测出未负载原纤维相对于负载原纤维的相对降解速率的差异。具体而言,我们发现SALS数据的偏心率呈线性增加,这与胶原纤维的优先保留和所施加的拉伸应变一致。我们得出的结论是,SALS简单,便宜,并且可以提供有用的光学筛选方法,允许对应变控制的组织和构建体进行实时监控。

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