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通过弛豫时间分布谱理解胶原基质的粘弹性行为。

Understanding the viscoelastic behavior of collagen matrices through relaxation time distribution spectrum.

作者信息

Xu Bin, Li Haiyue, Zhang Yanhang

机构信息

Department of Mechanical Engineering; Boston University; Boston, MA USA.

Department of Mechanical Engineering; Boston University; Boston, MA USA; Department of Biomedical Engineering; Boston University; Boston, MA USA.

出版信息

Biomatter. 2013 Jul-Sep;3(3). doi: 10.4161/biom.24651. Epub 2013 Apr 1.

Abstract

This study aims to provide understanding of the macroscopic viscoelastic behavior of collagen matrices through studying the relaxation time distribution spectrum obtained from stress relaxation tests. Hydrated collagen gel and dehydrated collagen thin film was exploited as two different hydration levels of collagen matrices. Genipin solution was used to induce crosslinking in collagen matrices. Biaxial stress relaxation tests were performed to characterize the viscoelastic behavior of collagen matrices. The rate of stress relaxation of both hydrated and dehydrated collagen matrices shows a linear initial stress level dependency. Increased crosslinking reduces viscosity in collagen gel, but the effect is negligible for thin film. Relaxation time distribution spectrum was obtained from the stress relaxation data by inverse Laplace transform. For most of the collagen matrices, three peaks at the short (0.3s ~1 s), medium (3s ~90 s), and long relaxation time (> 200 s) were observed in the continuous spectrum, which likely corresponds to relaxation mechanisms involve fiber, inter-fibril, and fibril sliding. Splitting of the middle peak was observed at higher initial stress levels suggesting increased structural heterogeneity at the fibril level with mechanical loading. The intensity of the long-term peaks increases with higher initial stress levels indicating the engagement of collagen fibrils at higher levels of tissue strain.

摘要

本研究旨在通过研究应力松弛试验获得的松弛时间分布谱,来深入了解胶原蛋白基质的宏观粘弹性行为。水合胶原蛋白凝胶和脱水胶原蛋白薄膜被用作胶原蛋白基质的两种不同水化水平。京尼平溶液用于诱导胶原蛋白基质中的交联。进行双轴应力松弛试验以表征胶原蛋白基质的粘弹性行为。水合和脱水胶原蛋白基质的应力松弛速率均显示出线性的初始应力水平依赖性。交联增加会降低胶原蛋白凝胶的粘度,但对薄膜的影响可忽略不计。通过拉普拉斯逆变换从应力松弛数据中获得松弛时间分布谱。对于大多数胶原蛋白基质,在连续谱中观察到短(0.3秒至1秒)、中(3秒至90秒)和长松弛时间(>200秒)处的三个峰,这可能对应于涉及纤维、纤维间和纤维滑动的松弛机制。在较高的初始应力水平下观察到中间峰的分裂,表明在机械加载下原纤维水平的结构异质性增加。长期峰的强度随着初始应力水平的升高而增加,表明在较高的组织应变水平下胶原蛋白原纤维的参与。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c786/3749280/c934b795ffd8/biom-3-e24651-g1.jpg

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