Accelerated Molecular Dynamics Study of the Effects of Surface Hydrophilicity on Protein Adsorption.
Accelerated Molecular Dynamics Study of the Effects of Surface Hydrophilicity on Protein Adsorption.
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DOI：
10.1021/acs.langmuir.6b02229
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发表时间：
2016-08
期刊：
影响因子：
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通讯作者：
Christian Mücksch;H. Urbassek
中科院分区：
文献类型：
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作者：
Christian Mücksch;H. Urbassek
链霉亲和素的吸附研究两个表面，石墨和二氧化钛，使用加速分子动力学。吸附在石墨上导致强烈的构象变化，而蛋白质在表面上展开。有趣的是，在高度亲水性的金红石表面上的吸附也引起蛋白质的相当大的扩散。我们把这种展开的原因归结为蛋白质与金红石表面上有序水层的相互作用。对于特殊的取向，蛋白质穿透有序的水层并与表面直接接触，其中带正电荷的氨基酸位于与带负电荷的金红石顶表面原子层相邻的位置。我们的结论是，对于研究的两种表面材料，链霉亲和素改变其构象如此强烈，它失去了结合生物素的潜力。我们的结果是在良好的定性协议与现有的实验研究。
The adsorption of streptavidin is studied on two surfaces, graphite and titanium dioxide, using accelerated molecular dynamics. Adsorption on graphite leads to strong conformational changes while the protein spreads out over the surface. Interestingly, also adsorption on the highly hydrophilic rutile surface induces considerable spreading of the protein. We pin down the cause for this unfolding to the interaction of the protein with the ordered water layers above the rutile surface. For special orientations, the protein penetrates the ordered water layers and comes into direct contact with the surface where the positively charged amino acids settle in places adjacent to the negatively charged top surface atom layer of rutile. We conclude that for both surface materials studied, streptavidin changes its conformation so strongly that it loses its potential for binding biotin. Our results are in good qualitative agreement with available experimental studies.