Fig. P1.

The self-assembly of hydrophobin proteins into a monolayer with rodlet morphology and amyloid characteristics. Hydrophobins are secreted by fungi as monomers. Upon encountering a hydrophobic:hydrophilic interface, such as the surface of a spore in contact with air, the structure of the hydrophobin monomer undergoes a change that results in the exposure of an aggregation-prone region. This region makes intermolecular contacts with adjacent monomers and forms the amyloid β-sheet core of the polymerized fibrillar structure. The remaining bulk of the protein is accommodated on the periphery of the rodlet. The rodlets pack together into an amphipathic monolayer that coats the spore surface and keeps it dry during dispersal in air.