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首页> 外文期刊>Physical chemistry chemical physics: PCCP >Amino acids and proteins at ZnO-water interfaces in molecular dynamics simulations
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Amino acids and proteins at ZnO-water interfaces in molecular dynamics simulations

机译：分子动力学模拟中ZnO-水界面的氨基酸和蛋白质

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We determine potentials of the mean force for interactions of amino acids with four common surfaces of ZnO in aqueous solutions. The method involves all-atom molecular dynamics simulations combined with the umbrella sampling technique. The profiled nature of the density of water with the strongly adsorbed first layer affects the approach of amino acids to the surface and generates either repulsion or weak binding. The largest binding energy is found for tyrosine interacting with the surface in which the Zn ions are at the top. It is equal to 7 kJ mol~(-1) which is comparable to that of the hydrogen bonds in a protein. This makes the adsorption of amino acids onto the ZnO surface much weaker than onto the well studied surface of gold. Under vacuum, binding energies are more than 40 times stronger (for one of the surfaces). The precise manner in which water molecules interact with a given surface influences the binding energies in a way that depends on the surface. Among the four considered surfaces the one with Zn at the top is recognized as binding almost all amino acids with an average binding energy of 2,60 kJ mol~(-1). Another (O at the top) is non-binding for most amino acids. For binding situations the average energy is 0.66 kJ mol~(-1). The remaining two surfaces bind nearly as many amino acids as they do not and the average binding energies are 1.46 and 1.22 kJ mol~(-1). For all of the surfaces the binding energies vary between amino acids significantly: the dispersion in the range of 68-154% of the mean. A small protein is shown to adsorb onto ZnO only intermittently and with only a small deformation. Various adsorption events lead to different patterns in mobilities of amino acids within the protein.
机译：我们确定在水溶液中氨基酸与ZnO的四个常见表面相互作用的平均力的潜力。该方法涉及与伞式采样技术相结合的全原子分子动力学模拟。具有高度吸附的第一层的水的密度的轮廓性质影响氨基酸到达表面的途径，并产生排斥或弱结合。发现酪氨酸与其中Zn离子在顶部的表面相互作用的最大结合能。它等于7 kJ mol〜（-1），与蛋白质中的氢键相当。这使得氨基酸在ZnO表面的吸附能力比在充分研究的金表面上弱得多。在真空下，结合能的强度（对于其中一个表面）要强40倍以上。水分子与给定表面相互作用的精确方式以取决于表面的方式影响结合能。在四个考虑的表面中，顶部带有Zn的表面被认为可以结合几乎所有氨基酸，平均结合能为2,60 kJ mol〜（-1）。另一个（顶部的O）与大多数氨基酸不结合。对于结合情况，平均能量为0.66 kJ mol〜（-1）。其余两个表面几乎与不结合的氨基酸结合，平均结合能为1.46和1.22 kJ mol〜（-1）。对于所有表面，氨基酸之间的结合能均显着变化：分散度在平均值的68-154％范围内。显示一种小的蛋白质仅间歇地且仅具有很小的变形才能吸附在ZnO上。各种吸附事件导致蛋白质内氨基酸迁移率的模式不同。

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