Interfaces and the driving force of hydrophobic assembly

  title={Interfaces and the driving force of hydrophobic assembly},
  author={David W. Chandler},
The hydrophobic effect — the tendency for oil and water to segregate — is important in diverse phenomena, from the cleaning of laundry, to the creation of micro-emulsions to make new materials, to the assembly of proteins into functional complexes. This effect is multifaceted depending on whether hydrophobic molecules are individually hydrated or driven to assemble into larger structures. Despite the basic principles underlying the hydrophobic effect being qualitatively well understood, only… 

Measurement of the Hydrophobic Force in a Soft Matter System.

By studying the interaction between two hydrophobic oil drops in water under well-controlled conditions where all known surface forces are suppressed, this work observes only a strong, short-ranged attraction with an exponential decay length of 0.30 ± 0.03 nm, comparable to molecular correlations of water molecules.

Supramolecular Assembly and Binding in Aqueous Solution: Useful Tips Regarding the Hofmeister and Hydrophobic Effects

The self-assembly of structurally discrete entities, and supramolecular chemistry in general, continues to expand into the aqueous realm. To do so, however, requires a firm understanding of the

Role of molecular architecture in the modulation of hydrophobic interactions

Bubble formation in nanopores: a matter of hydrophobicity, geometry, and size

ABSTRACT This review focuses on the phase behaviour of liquids in nanoscale confinement, which promotes drying by a combination of hydrophobicity, small size, and high degree of confinement. In these

Charge, hydrophobicity, and confined water: putting past simulations into a simple theoretical framework.

This work presents a simple statistical mechanical model for the forces water mediates between different confining surfaces, and demonstrates that the model qualitatively unifies a wide range of phenomena known in the simulation literature, including several cases of protein folding under confinement.

Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forces

Standard nonpolarizable force fields used in classical simulations are capable of resolving the fine details of the hydrophobic attraction of peptides, and analysis of the involved energetics shows that water-structure effects and dispersive interactions give contributions of comparable magnitude that largely cancel out.

Hydrophobic Surface Engineering for the Construction of Discrete Aggregates

Exactly defined number of gear-shaped amphiphiles self-assemble into discrete aggregates. In water (or aqueous methanol) these amphiphiles mesh each other so as to reduce indented hydrophobic surface

A minireview on the perturbation effects of polar groups to direct nanoscale hydrophobic interaction and amphiphilic peptide assembly

This review aims to outline the recent efforts made to determine the hydrophobic interaction at a nanoscopic length scale and discusses the influence of chemical heterogeneity on the modulation of amphiphilic peptide/protein assembly and molecular recognition.

Length-Scale Effects in Hydrophobic Polymer Collapse Transitions.

The role of length scales in polymer solubility problems is discussed and new ideas on surfactant mechanisms are discussed based on examples in which these mechanisms drive polymer swelling or collapse.

Comparative Study of Water-Mediated Interactions between Hydrophilic and Hydrophobic Nanoscale Surfaces.

The results suggest that the forces between hydrophobic, hydrophilic, hydphobic/hydrophilic surfaces are all relevant in driving a self-assembly system towards its final state but it is thehydrophobic interaction that provides stability to such a final state.



Micelle Formation and the Hydrophobic Effect

The tendency of amphiphilic molecules to form micelles in aqueous solution is a consequence of the hydrophobic effect. The fundamental difference between micelle assembly and macroscopic phase

Drying-induced hydrophobic polymer collapse

We have used computer simulation to study the collapse of a hydrophobic chain in water. We find that the mechanism of collapse is much like that of a first-order phase transition. The evaporation of

Assembly of extended interfaces and micelles: charge frustrated models of amphiphilic mixtures

This paper describes aspects of self-assembly in complex fluids in terms of the concept of charge frustration. This concept follows from the analogy between electrostatic energy and the entropic

Hydrophobicity at a Janus Interface

Water confined between adjoining hydrophobic and hydrophilic surfaces (a Janus interface) is found to form stable films of nanometer thickness whose responses to shear deformations are extraordinarily noisy, indicating a distribution of relaxation processes rather than any dominant one.

The hydrophobic effect and the organization of living matter.

Biological organization may be viewed as consisting of two stages: biosynthesis and assembly; that is, as a first approximation it represents a search by each structural molecule for its state of lowest chemical potential.

Interfacial free energy and the hydrophobic effect.

  • C. Tanford
  • Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1979
The discrepancy inacial free energies illustrates the difficulty in applying macroscopic concepts such as "interfacial surface" at the molecular level and can be formally resolved, at least qualitatively, by the predicted effect of surface curvature on surface tension.

Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects.

Alkane solubility data have been reevaluated to account for solute-solvent size differences, leading to a revised "microscopic" hydrophobic effect of 47 cal mol-1 A-2, which predicts a macroscopic alkane-water surface tension that is close to the macroscopy value.

Quantification of the hydrophobic interaction by simulations of the aggregation of small hydrophobic solutes in water

This is the first direct calculation, to the authors' knowledge, of the hydrophobic interaction from molecular dynamics simulations; the excellent qualitative and quantitative agreement with experiment proves that simple van der Waals interactions and atomic point-charge electrostatics account for the most important driving force in biology.


Measurements of the forces in water between neutral hydrophobic surfaces prepared by covalent modification of glass are presented. The surfaces are stable under a variety of conditions including high

The hydrophobic effect and the influence of solute-solvent attractions

We have studied the effect of weak solute−solvent attractions on the solvation of nonpolar molecules in water at ambient conditions using an extension and improved parameterization of the theory of