跟腱
胶原纤维
粘弹性
纤维
肌腱
纳米尺度
材料科学
应力松弛
拉伤
生物物理学
放松(心理学)
变形(气象学)
表征(材料科学)
生物医学工程
复合材料
解剖
纳米技术
医学
蠕动
内科学
生物
作者
Isabella Silva Barreto,Maria Pierantoni,Malin Hammerman,Elin Törnquist,Sophie Le Cann,Ana Díaz,Jonas Engqvist,Marianne Liebi,Pernilla Eliasson,Hanna Isaksson
标识
DOI:10.1016/j.matbio.2022.11.006
摘要
The specific viscoelastic mechanical properties of Achilles tendons are highly dependent on the structural characteristics of collagen at and between all hierarchical levels. Research has been conducted on the deformation mechanisms of positional tendons and single fibrils, but knowledge about the coupling between the whole tendon and nanoscale deformation mechanisms of more commonly injured energy-storing tendons, such as Achilles tendons, remains sparse. By exploiting the highly periodic arrangement of tendons at the nanoscale, in situ loading of rat Achilles tendons during small-angle X-ray scattering acquisition was used to investigate the collagen structural response during load to rupture, cyclic loading and stress relaxation. The fibril strain was substantially lower than the applied tissue strain. The fibrils strained linearly in the elastic region of the tissue, but also exhibited viscoelastic properties, such as an increased stretchability and recovery during cyclic loading and fibril strain relaxation during tissue stress relaxation. We demonstrate that the changes in the width of the collagen reflections could be attributed to strain heterogeneity and not changes in size of the coherently diffracting domains. Fibril strain heterogeneity increased with applied loads and after the toe region, fibrils also became increasingly disordered. Additionally, a thorough evaluation of radiation damage was performed. In conclusion, this study clearly displays the simultaneous structural response and adaption of the collagen fibrils to the applied tissue loads and provide novel information about the transition of loads between length scales in the Achilles tendon.
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