Adsorption of Collagen Nanofibrils on Rough TiO2: A Molecular Dynamics Study
Adsorption of Collagen Nanofibrils on Rough TiO2: A Molecular Dynamics Study
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DOI：
10.1002/adem.201080123
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发表时间：
2011-10
影响因子：
3.6
通讯作者：
W. Friedrichs;B. Ohler;W. Langel;S. Monti;S. Köppen
中科院分区：
文献类型：
--
作者：
W. Friedrichs;B. Ohler;W. Langel;S. Monti;S. Köppen
经典的分子动力学模拟粗糙的二氧化钛表面的原胶原分子。在平面金红石（100）的基础上，采用了两种表面粗糙度模型：（1 × 3）尺寸小于14 μ m的微面对直径约为16 μ m的三螺旋结构的吸附影响很小。在增加粗糙度后，观察到螺旋结合的空间位阻。开发了胶原三螺旋的端肽加帽模型。高度灵活的端肽结构介导的表面上的吸附和插入到两个表面模型的凹槽。原胶原C末端的端肽β转角基序与三螺旋的特异性受体区域相互作用。这一分子间过程似乎是熵驱动的，可能是螺旋组装成有序原纤维的第一步。端肽和三螺旋之间的相互作用似乎是在竞争，而焓控制的表面吸附的单个胶原分子。
Classical molecular dynamics simulations of tropocollagen molecules on rough titania surfaces are presented. On the basis of plane rutile (100), two models for surface roughness have been adopted: (1 × 3) microfacets with dimensions of less than 14 Å had only minor influence on the adsorption of a triple helical structure with a diameter of about 16 Å. After increasing the roughness by terraces, steric hindrance of helix binding was observed. A model for telopeptide capping of the collagen triple helices was developed. The highly flexible telopeptide structures mediated adsorption on the surface and inserted into grooves of both surface models. The telopeptide β‐turn motifs at the C‐terminus of the tropocollagen interact with specific receptor regions of the triple helices. This intermolecular process seems to be entropy driven and may be the first step of assembling helices to ordered fibrils. Interaction between telopeptide and triple helix seems to be in competition with the rather enthalpy controlled surface adsorption of single collagen molecules.