Competing adsorption between hydrated peptides and water onto metal surfaces: From electronic to conformational properties
Competing adsorption between hydrated peptides and water onto metal surfaces: From electronic to conformational properties
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DOI：
10.1021/ja804350v
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发表时间：
2008-10-08
影响因子：
15
通讯作者：
Delle Site, Luigi
中科院分区：
文献类型：
--
作者：
Ghiringhelli, Luca M.;Hess, Berk;Delle Site, Luigi
无机-（生物）有机界面在当前研究的许多领域中具有核心重要性。理论和计算工具面临着不同的时间和长度尺度的困难问题，涉及并以非平凡的方式联系在一起。在这项工作中，最近提出的分级量子经典尺度桥接方法进一步发展，以研究大的柔性分子。然后，该方法被应用于研究在完全润湿条件下的亲水性Pt（111）表面上的寡肽的吸附。我们研究组氨酸序列，这是众所周知的，其结合亲和力的金属表面。基于与苯丙氨酸的比较，其结合强组氨酸在高真空条件下，但我们发现，在潮湿条件下没有表面亲和力，我们说明了近表面水分子的介导作用。这些对肽结合的机制和强度有显著贡献。除了提供表面结合机制的物理化学见解，我们的计算方法为表面特异性序列设计提供了未来的机会。
Inorganic-(bio)organic interfaces are of central importance in many fields of current research. Theoretical and computational tools face the difficult problem of the different time and length scales that are involved and linked in a nontrivial way. In this work, a recently proposed hierarchical quantum-classical scale-bridging approach is further developed to study large flexible molecules. The approach is then applied to study the adsorption of oligopeptides on a hydrophilic Pt(111) surface under complete wetting conditions. We examine histidine sequences, which are well known for their binding affinity to metal surfaces. Based on a comparison with phenylalanine, which binds as strong as histidine under high vacuum conditions but, as we show, has no surface affinity under wet conditions, we illustrate the mediating effects of near-surface water molecules. These contribute significantly to the mechanism and strength of peptide binding. In addition to providing physical-chemical insights in the mechanism of surface binding, our computational approach provides future opportunities for surface-specific sequence design.