Interaction of Amino Acids with the Au(111) Surface: Adsorption Free Energies from Molecular Dynamics Simulations
Interaction of Amino Acids with the Au(111) Surface: Adsorption Free Energies from Molecular Dynamics Simulations
复制标题
DOI：
10.1021/la904765u
复制
发表时间：
2010-06-01
期刊：
影响因子：
3.9
通讯作者：
Gottschalk, Kay-Eberhard
中科院分区：
文献类型：
--
作者：
Hoefling, Martin;Iori, Francesco;Gottschalk, Kay-Eberhard
蛋白质与无机表面的相互作用在生物事件和现代生物技术应用中具有高度重要性。因此，肽已被工程化以高特异性识别无机表面。然而，基本的相互作用仍然没有得到很好的理解。在这里，我们研究了吸附的氨基酸作为蛋白质积木上的Au（111）表面。特别是，使用分子动力学模拟，我们计算了所有20个氨基酸和旧表面之间的平均力的潜力。我们发现一个强烈的依赖性的结合亲和力的氨基酸的化学性质。另外。相互作用自由能与氨基酸形成β-折叠的倾向相关，暗示了旧结合肽的设计原理和在表面附近诱导β-折叠形成。
Interactions of proteins with inorganic surfaces are of high importance in biological events and in modern biotechnological applications. Therefore, peptides have been engineered to recognize inorganic surfaces with high specificity. However, the underlying interactions are still not well understood. Here, we investigated the adsorption of amino acids as protein building blocks onto a Au(111) surface. In particular, using molecular dynamics simulations, we calculated the potential of mean force between all the 20 amino acids and the old surface. We found a strong dependence of the binding affinities on the chemical character of the amino acids. Additionally. the interaction free energy is correlated with the propensity of amino acids to form beta-sheets, hinting at design principles for old binding peptides and induction of beta-sheet formation near surfaces.