Hydrophobic Interactions and Dewetting between Plates with Hydrophobic and Hydrophilic Domains

TL;DR

This study uses molecular dynamics simulations to explore how the distribution of hydrophobic and hydrophilic domains on plates influences wetting, dewetting, and hydrophobic interactions, revealing complex cooperative effects.

Contribution

It demonstrates that the spatial arrangement of surface domains critically affects dewetting transitions and hydrophobic interactions, challenging the assumption of additivity in such interactions.

Findings

Large hydrophobic domains induce dewetting and attraction.

Homogeneous distributions prevent dewetting and cause repulsion.

Janus interfaces remain wet until steric constraints eject water.

Abstract

We study by molecular dynamics simulations the wetting/dewetting transition and the dependence of the free energy on distance between plates that contain both hydrophobic and hydrophilic particles. We show that dewetting and strength of hydrophobic interaction is very sensitive to the distribution of hydrophobic and hydrophilic domains. In particular, we find that plates characterized by a large domain of hydrophobic sites induce a dewetting transition and an attractive solvent-induced interaction. On the other hand, a homogeneous distribution of the hydrophobic and hydrophilic particles on the plates prevents the dewetting transition and produces a repulsive solvent-induced interaction. We also present results for a kind of Janus interface in which one plate consists of hydrophobic particles and the other of hydrophilic particles showing that the inter-plate gap remains wet until steric constraints at small separations eject the water molecules. Our results indicate that the Cassie equation, for the contact angle of a heterogeneous plate, can not be used to predict the critical distance of dewetting. These results indicate that hydrophobic interactions between nanoscale surfaces with strong large length-scale hydrophobicity can be highly cooperative and thus they argue against additivity of the hydrophobic interactions between different surface domains in these cases. These findings are pertinent to certain protein-protein interactions where additivity is commonly assumed.