Jerzy Haber Institute of Catalysis and Surface Chemistry (PAS) , Niezapominajek 8 , 30-239 Cracow , Poland.
Department of Chemical and Process Engineering , University of Strathclyde , James Weir Building, 75 Montrose Street , G1 1XJ Glasgow , U.K.
J Phys Chem B. 2018 Apr 12;122(14):3744-3753. doi: 10.1021/acs.jpcb.7b12484. Epub 2018 Mar 28.
We study the energy landscape of the negatively charged protein bovine serum albumin adsorbed on a negatively charged silica surface at pH 7. We use fully atomistic molecular dynamics (MD) and steered MD (SMD) to probe the energy of adsorption and the pathway for the surface diffusion of the protein and its associated activation energy. We find an adsorption energy ∼1.2 eV, which implies that adsorption is irreversible even on experimental time scales of hours. In contrast, the activation energy for surface diffusion is ∼0.4 eV so that it is observable on the MD simulation time scale of 100 ns. This analysis paves the way for a more detailed understanding of how a protein layer forms on biomaterial surfaces, even when the protein and surface share the same electrical polarity.
我们研究了在 pH 值为 7 时带负电荷的牛血清白蛋白蛋白吸附在带负电荷的硅胶表面上的能量景观。我们使用全原子分子动力学（MD）和导向 MD（SMD）来探测蛋白的吸附能和其表面扩散的途径以及相关的活化能。我们发现吸附能约为 1.2 eV，这意味着即使在实验时间尺度为小时的情况下，吸附也是不可逆的。相比之下，表面扩散的活化能约为 0.4 eV，因此在 100 ns 的 MD 模拟时间尺度上是可以观察到的。这种分析为更详细地了解蛋白质层如何在生物材料表面形成铺平了道路，即使蛋白质和表面具有相同的极性。
