Faceted particles formed by the frustrated packing of anisotropic colloids on curved surfaces.

We use computer simulations and simple theoretical models to analyze the morphologies that result when rod-like particles end-attach onto a curved surface, creating a finite-thickness monolayer aligned with the surface normal. This geometry leads to two forms of frustration, one associated with the incompatibility of hexagonal order on surfaces with Gaussian curvature, and the second reflecting the deformation of a layer with finite thickness on a surface with non-zero mean curvature. We show that the latter effect leads to a faceting mechanism. Above threshold values of inter-particle attraction strength and surface mean curvature, the adsorbed layer undergoes a transition from orientational disorder to an ordered state that is demarcated by reproducible patterns of line defects. The number of facets is controlled by the competition between line defect energy and intra-facet strain. Tuning control parameters thus leads to a rich variety of morphologies, including icosahedral particles and irregular polyhedra. In addition to suggesting a new strategy for the synthesis of aspherical particles with tunable symmetries, our results may shed light on recent experiments in which rod-like HIV GAG proteins assemble around nanoscale particles.

Simulations of HIV capsid protein dimerization reveal the effect of chemistry and topography on the mechanism of hydrophobic protein association.

Recent work has shown that the hydrophobic protein surfaces in aqueous solution sit near a drying transition. The tendency for these surfaces to expel water from their vicinity leads to self-assembly of macromolecular complexes. In this article, we show with a realistic model for a biologically pertinent system how this phenomenon appears at the molecular level. We focus on the association of the C-terminal domain (CA-C) of the human immunodeficiency virus capsid protein. By combining all-atom simulations with specialized sampling techniques, we measure the water density distribution during the approach of two CA-C proteins as a function of separation and amino acid sequence in the interfacial region. The simulations demonstrate that CA-C protein-protein interactions sit at the edge of a dewetting transition and that this mesoscopic manifestation of the underlying liquid-vapor phase transition can be readily manipulated by biology or protein engineering to significantly affect association behavior. Although the wild-type protein remains wet until contact, we identify a set of in silico mutations, in which three hydrophilic amino acids are replaced with nonpolar residues, that leads to dewetting before association. The existence of dewetting depends on the size and relative locations of substituted residues separated by nanometer length scales, indicating long-range cooperativity and a sensitivity to surface topography. These observations identify important details that are missing from descriptions of protein association based on buried hydrophobic surface area.