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首页> 外文期刊>Journal of Applied Polymer Science >Transition from Viscous to Elastic-Based Dependency of Mechanical Properties of Self-Assembled Type I Collagen Fibers
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Transition from Viscous to Elastic-Based Dependency of Mechanical Properties of Self-Assembled Type I Collagen Fibers

机译:自组装的I型胶原纤维的机械性能从粘性转变为基于弹性的依赖关系

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Fibrous collagen networks are the major elements that provide mechanical integrity to tissues; they are composed of fiber forming collagens in combination with proteoglycans and elastic fibers. Using uniaxial incremental tensile stress-strain tests we have studied the viscoelastic mechanical properties of self -assembled collagen fibers formed at pHs between 5.5 and 8.5 and temperatures of25 and 37°C. Fibers formed at pH 7.5 and 37°C and crosslinked by aging at 22°C and 1 atmosphere pressure were also tested. Analysis of the mechanical tests showed that the ultimate tensile strength CUTS), and slopes of the total, elastic and viscous stress-strain curves were related directly to the volume fraction of polymer. Further analysis suggested that the UTS, and slopes of the total, elastic, and viscous stress-strain curves showed the highest correlation coefficient with the calculated effective fibril length and axial ratio. The mechanical data suggested that at low levels of crosslinking the mechanical properties were dominated by the viscous sliding of collagen molecules and fibrils by each other , which appears to be dependent on the collagen fibril length and axial ratio, while at higher levels of crosslinking the mechanical behavior is dominated by elastic stretching of the nonhelicalends, crosslinks, and collagen triple helix. The latter behavior appears to be dependent on the presence ofcrosslinks that stabilize fibrillar units. These results lead to the hypothesis that early in development viscous sliding of fibrils plays an important role in the mechanical response of animal tissues to forces experienced in Iltero, while later in development when locomotion is required, mechanical stability is primarily a result of elastic deformation of the different parts of the collagen molecule within crosslinked fibrils.
机译:纤维胶原蛋白网络是提供组织机械完整性的主要元素。它们由形成纤维的胶原蛋白,蛋白聚糖和弹性纤维组成。使用单轴增量拉伸应力应变测试,我们研究了在5.5至8.5的pH和25至37°C的温度下形成的自组装胶原纤维的粘弹性力学性能。还测试了在pH 7.5和37°C下形成并通过在22°C和1个大气压下老化而交联的纤维。力学测试的分析表明,极限拉伸强度(CUTS)以及总应力,弹性应力和粘性应力-应变曲线的斜率与聚合物的体积分数直接相关。进一步的分析表明,UTS以及总应力,弹性应力和粘性应力-应变曲线的斜率与计算出的有效原纤维长度和轴向比显示出最高的相关系数。力学数据表明,在低交联水平下,机械性能主要由胶原分子和原纤维彼此之间的粘性滑动决定,这似乎取决于胶原原纤维的长度和轴向比,而在较高交联水平下,机械性能高。行为主要由非螺旋末端,交联和胶原三螺旋的弹性拉伸决定。后者的行为似乎取决于稳定原纤维单元的交联的存在。这些结果导致这样的假设,即发育初期的纤维原状粘性滑动在动物组织对Iltero所经历的力的机械反应中起着重要作用,而在后来的发展中,当需要运动时,机械稳定性主要是由于弹性变形引起的。交联原纤维中胶原蛋白分子的不同部分。

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