Molecular dynamic simulations of hydrophobins: pure-protein bilayers and lipid-protein interactions

Abstract

Hydrophobins are a family of proteins characterized by a large exposed hydrophobic region, rendering them highly amphiphilic. Class II hydrophobins such as HFBI self-assemble into monolayers at water-air or water-oil interfaces, revealing long-range ordered hexagonal ‘honeycomb’ structures[1]. This property allows for the preparation of pure-protein bilayers and vesicles [2] with unexpectedly low permeability for water and ions. To provide a molecular explanation for these properties, we carried out atomistic and coarse grained molecular dynamics (MD) simulations of HFBI bilayers.