Preferred orientation of albumin adsorption on a hydrophilic surface from molecular simulation
Preferred orientation of albumin adsorption on a hydrophilic surface from molecular simulation
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DOI：
10.1016/j.colsurfb.2008.08.017
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发表时间：
2008-12-01
影响因子：
5.8
通讯作者：
Tsay, Ruey-Yug
中科院分区：
文献类型：
--
作者：
Hsu, Hao-Jen;Sheu, Sheh-Yi;Tsay, Ruey-Yug
一般来说，非特异性蛋白质吸附遵循两步程序，即首先以天然形式吸附到表面上，随后在表面上发生构象变化。为了预测随后的构象变化，重要的是在吸附的第一步中确定吸附的蛋白质的优选取向。在这项工作中，一种方法的基础上找到全局最小的相互作用势能的吸附蛋白质已被开发来描绘的人血清白蛋白（HSA）油的模型表面的亲水性自组装单分子层（SAM）的吸附的优选取向。为了计算效率，溶剂化效应被大大简化，只包括静电效应的阻尼，而忽略了由于水分子对表面上的官能团的竞争的贡献。通过分子的系统旋转结合与表面的垂直运动获得的等高线图给出了吸附分子在各种吸附取向下的最小相互作用能。模拟结果表明，对于-OH封端的SAM表面，HSA的“背对”取向是优选取向。这种吸附取向的投影面积对应于心形HSA分子的“三角形侧对”吸附。本文提出的方法是能够提供的结果是一致的Monte Carlo（MC）模拟预测的计算成本大大降低。当前方法的高计算效率使其有可能被实现为用于控制表面上蛋白质吸附的设计工具;然而。在完全实现这一点之前，必须进一步发展这些方法，以便能够计算相互作用自由能来代替势能，同时沿着更真实地表示溶剂化效应。(C)2008 Elsevier B. V.保留所有权利。
In general, non-specific protein adsorption follows a two-step procedure, i.e. first adsorption onto a Surface in native form, and a subsequent conformational change oil the surface. In order to predict the subsequent conformational change, it is important to determine the preferred orientation of an adsorbed protein in the first step of the adsorption. In this work, a method based on finding the global minimum of the interaction potential energy of an adsorbed protein has been developed to delineate the preferred orientations for the adsorption of human serum albumin (HSA) oil a model surface with a hydrophilic self-assembled monolayer(SAM). For computational efficiency,solvation effects were greatly simplified by only including the dampening of electrostatic effects while neglecting contributions due to the competition of water molecules for the functional groups on the surface. A contour map obtained by systematic rotation of a molecule in conjunction with perpendicular motion to the surface gives the minimum interaction energy of the adsorbed molecule at various adsorption orientations. Simulation results show that for an -OH terminated SAM Surface, a "back-on" orientation of HSA is the preferred orientation. The projection area of this adsorption orientation Corresponds with the "triangular-side-on" adsorption of a heart shaped HSA molecule. The method proposed herein is able to provide results which are consistent with those predicted by Monte Carlo (MC) simulations with a substantially less computing cost. The high Computing efficiency of the current method makes it possible to be implemented as a design tool for the control of Protein adsorption On Surfaces; however. before this can be fully realized, these methods must be further developed to enable interaction free energy to be calculated in place of potential energy, along with a more realistic representation of solvation effects. (C) 2008 Elsevier B.V. All rights reserved.