Howard P Isermann Department of Chemical and Biological Engineering, and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):17678-83. doi: 10.1073/pnas.1110703108. Epub 2011 Oct 10.
Interfaces are a most common motif in complex systems. To understand how the presence of interfaces affects hydrophobic phenomena, we use molecular simulations and theory to study hydration of solutes at interfaces. The solutes range in size from subnanometer to a few nanometers. The interfaces are self-assembled monolayers with a range of chemistries, from hydrophilic to hydrophobic. We show that the driving force for assembly in the vicinity of a hydrophobic surface is weaker than that in bulk water and decreases with increasing temperature, in contrast to that in the bulk. We explain these distinct features in terms of an interplay between interfacial fluctuations and excluded volume effects--the physics encoded in Lum-Chandler-Weeks theory [Lum K, Chandler D, Weeks JD (1999) J Phys Chem B 103:4570-4577]. Our results suggest a catalytic role for hydrophobic interfaces in the unfolding of proteins, for example, in the interior of chaperonins and in amyloid formation.
界面是复杂系统中最常见的主题。为了了解界面的存在如何影响疏水性现象，我们使用分子模拟和理论来研究溶质在界面处的水合作用。溶质的大小范围从亚纳米到几个纳米。界面是自组装单层，具有从亲水到疏水的各种化学性质。我们表明，在疏水表面附近组装的驱动力比在本体水中弱，并且随着温度的升高而降低，这与在本体中的情况相反。我们根据界面波动和排除体积效应之间的相互作用来解释这些明显的特征——Lum-Chandler-Weeks 理论中所包含的物理原理[Lum K、Chandler D、Weeks JD（1999）J Phys Chem B 103:4570-4577]。我们的结果表明，疏水界面在蛋白质的展开中具有催化作用，例如，在伴侣蛋白的内部和淀粉样蛋白的形成中。
