Investigation on the behavior of collagen self-assembly in vitro via adding sodium silicate.
Investigation on the behavior of collagen self-assembly in vitro via adding sodium silicate.
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DOI：
10.1016/j.ijbiomac.2018.04.074
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发表时间：
2018-04
影响因子：
8.2
通讯作者：
Lirui Shen;Honghong Bu;Huan Yang;Wentao Liu;Guoying Li
中科院分区：
文献类型：
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作者：
Lirui Shen;Honghong Bu;Huan Yang;Wentao Liu;Guoying Li
硅是人体内发现的一种微量元素，在胶原蛋白自组装过程中起着至关重要的作用。在本研究中，研究了分子间相互作用和原纤维形成过程，以了解不同浓度的硅酸钠（SS）对胶原体外自组装的影响。傅里叶变换红外光谱分析表明，SS对胶原蛋白的三螺旋结构没有显着影响。使用芘荧光和动态光扫描测量胶原蛋白聚集体的疏水相互作用和粒径，通过添加 2mM SS 得到增强，而随着浓度的进一步增加 (4-8mM) 而减小。动力学分析表明，在 2mM SS 存在的情况下，疏水相互作用的增加促进了胶原蛋白的自组装。添加 4-8mM SS 对自组装的抑制，如原纤维形成率和浊度的降低所示，可能归因于弱疏水相互作用和强静电排斥。显微镜观察表明，原纤维在 2mM SS 下表现出特征性的 D 周期性。 4mM SS 的抑制作用轻微，仍形成原纤维，而当 SS≥6mM 时，由于严重抑制胶原自组装，微观结构由簇状胶原聚集体组成。
Silicon, a trace element found in human body, plays a critical role in the process of collagen self-assembly. In this study, the intermolecular interaction and fibrillogenesis process were investigated to understand the effects of various concentrations of sodium silicate (SS) on collagen self-assemblyin vitro. Fourier transform infrared spectroscopy analysis indicated that the triple helical structure of collagen was not significantly affected by SS. Hydrophobic interactions and particle sizes of collagen aggregates, which were measured using pyrene fluorescence and dynamic light scanning, enhanced via adding 2 mM SS whereas decreased with further increasing concentrations (4–8 mM). Kinetic analysis revealed that an increase in hydrophobic interactions boosted collagen self-assembly in the presence of 2 mM SS. The inhibition of self-assembly with the addition of 4–8 mM SS, as illustrated by a reduction in the fibrillogenesis rate and turbidity, was potentially attributed to weak hydrophobic interactions and strong electrostatic repulsion. The observation of microscopy demonstrated that the fibrils exhibited the characteristic D-periodicity at 2 mM SS. The inhibitory effect of 4 mM SS was slight and the fibrils still formed, while the microstructure was consisted of clustered collagen aggregates as SS ≥ 6 mM owing to serious inhibition on collagen self-assembly.