amino acid
; carbon nanotube
; hydrophobin
; hydroxyl group
; methyl group
; nanomaterial
; water
; graphite
; nanotube
; solvent
; Article
; cell adhesion
; controlled study
; energy transfer
; hydration
; hydrogen bond
; hydrophilicity
; hydrophobicity
; molecular dynamics
; nonhuman
; priority journal
; protein structure
; surface area
; surface property
; topography
; wettability
; chemical phenomena
; chemistry
; human
; metabolism
; molecular dynamics
; protein conformation
; Graphite
; Humans
; Hydrophobic and Hydrophilic Interactions
; Molecular Dynamics Simulation
; Nanotubes
; Protein Conformation
; Solvents
; Water
英文摘要:
Hydrophobic interactions drive many important biomolecular self-assembly phenomena. However, characterizing hydrophobicity at the nanoscale has remained a challenge due to its nontrivial dependence on the chemistry and topography of biomolecular surfaces. Here we use molecular simulations coupled with enhanced sampling methods to systematically displace water molecules from the hydration shells of nanostructured solutes and calculate the free energetics of interfacial water density fluctuations, which quantify the extent of solute-water adhesion, and therefore solute hydrophobicity. In particular, we characterize the hydrophobicity of curved graphene sheets, self-assembled monolayers (SAMs) with chemical patterns, and mutants of the protein hydrophobin-II. We find that water density fluctuations are enhanced near concave nonpolar surfaces compared with those near flat or convex ones, suggesting that concave surfaces are more hydrophobic. We also find that patterned SAMs and protein mutants, having the same number of nonpolar and polar sites but different geometrical arrangements, can display significantly different strengths of adhesion with water. Specifically, hydroxyl groups reduce the hydrophobicity of methyl-terminated SAMs most effectively not when they are clustered together but when they are separated by one methyl group. Hydrophobin-II mutants show that a charged amino acid reduces the hydrophobicity of a large nonpolar patch when placed at its center, rather than at its edge. Our results highlight the power of water density fluctuations-based measures to characterize the hydrophobicity of nanoscale surfaces and caution against the use of additive approximations, such as the commonly used surface area models or hydropathy scales for characterizing biomolecular hydrophobicity and the associated driving forces of assembly.
Xi, E., Department of Chemical and Biomolecular Engineering, University of Pennsylvania, Philadelphia, PA 19104, United States; Venkateshwaran, V., Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, United States, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; Li, L., Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, United States, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; Rego, N., Department of Chemical and Biomolecular Engineering, University of Pennsylvania, Philadelphia, PA 19104, United States; Patel, A.J., Department of Chemical and Biomolecular Engineering, University of Pennsylvania, Philadelphia, PA 19104, United States; Garde, S., Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, United States, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; Klein, M.L., Temple University, Philadelphia, PA, United States
Recommended Citation:
Xi E.,Venkateshwaran V.,Li L.,et al. Hydrophobicity of proteins and nanostructured solutes is governed by topographical and chemical context[J]. Proceedings of the National Academy of Sciences of the United States of America,2017-01-01,114(51)