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In vitro fibrillogenesis of tropocollagen type III in collagen type I affects its relative fibrillar topology and mechanics

机译:I型胶原中III型原胶原蛋白的体外原纤维形成影响其相对原纤维的拓扑结构和力学

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摘要

Tropocollagen types I and III were simultaneously fibrilized in vitro, and the differences between the geometric and mechanical properties of the heterotypic fibrils with different mixing ratios of tropocollagen III to I were investigated. Transmission electron microscopy was used to confirm the simultaneous presence of both tropocollagen types within the heterotypic fibrils. The incorporation of collagen III in I caused the fibrils to be thinner with a shorter D-banding than pure collagen I. Hertzian contact model was used to obtain the elastic moduli from atomic force microscope indentation testing using a force volume analysis. The results indicated that an increase in the percentage of tropocollagen III reduced the mechanical stiffness of the obtained fibrils. The mechanical stiffness of the collagen fibrils was found to be greater at higher loading frequencies. This observation might explain the dominance of collagen III over I in soft distensible organs such as human vocal folds.
机译:将I型和III型胶原蛋白在体外同时原纤化,并研究了不同比例的原胶原蛋白III与I混合的异型原纤维的几何和机械性能之间的差异。使用透射电子显微镜确认异型原纤维中两种对流胶原蛋白类型的同时存在。与纯胶原蛋白I相比,胶原蛋白III在I中的掺入使原纤维更薄,D带更短。赫兹接触模型用于通过力体积分析从原子力显微镜压痕测试获得弹性模量。结果表明,原胶原蛋白III的百分比的增加降低了获得的原纤维的机械刚度。发现胶原纤维的机械刚度在较高的加载频率下更大。该观察结果可以解释在人的声带等软性可扩张器官中,III型胶原蛋白占主导地位。

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