title: Extended surfaces modulate hydrophobic interactions of neighboring solutes.
abstract: 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.
authors: Howard P Isermann Department of Chemical and Biological Engineering, and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
authors: Amish J
authors: AJ
authors: Patel
authors: Patrick
authors: P
authors: Varilly
authors: Sumanth N
authors: SN
authors: Jamadagni
authors: Hari
authors: H
authors: Acharya
authors: Shekhar
authors: S
authors: Garde
authors: David
authors: D
authors: Chandler
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D056004:Molecular Dynamics Simulation; D011506:Proteins / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry*; D013499:Surface Properties; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D012996:Solutions; D014867:Water