Proteins from the hydrophobin family are produced by filamentous fungi in a soluble form, which spontaneously self-assemble at air/water or hydrophobic/hydrophilic interfaces to produce amphipathic layers and accomplish their biological role. Hydrophobin layers consist of rodlets that show the hallmarks of protein amyloids. Hydrophobins are thus functional amyloids that self-organise into well-ordered layers with remarkable physicochemical properties. The FUNHYDRO project is centred on the hydrophobin functional amyloids from the opportunistic pathogen Aspergillus fumigatus. This fungus has become the major airborne human fungal pathogen, causing severe diseases in immunocompromised individuals leading to over 200000 deaths per year worldwide. The A. fumigatus spores are coated with a hydrophobic rodlet layer made by the RodA hydrophobin, which protects the spores against desiccation, facilitates their dispersal in the air and renders the spores inert relative to the immune system. The aim of this ambitious proposal is to characterise in depth the self-assembly, structure and interactions with cell wall components (CWC) of hydrophobin amyloids from the airborne pathogen Aspergillus fumigatus.