title: Formation of amphipathic amyloid monolayers from fungal hydrophobin proteins.
abstract: The fungal hydrophobins are small proteins that are able to spontaneously self-assemble into amphipathic monolayers at hydrophobic:hydrophilic interfaces. These protein monolayers can reverse the wettability of a surface, making them suitable for increasing the biocompatibility of many hydrophobic nanomaterials. One subgroup of this family, the class I hydrophobins, forms monolayers that are composed of extremely robust amyloid-like fibrils, called rodlets. Here we describe protocols for the production and purification of recombinant hydrophobins and oxidative refolding to a biologically active, soluble, monomeric form. We describe methods to trigger self-assembly into the fibrillar rodlet state and techniques to characterize the physicochemical properties of the polymeric forms.
authors.affiliation: School of Molecular Bioscience and Discipline of Pharmacology, University of Sydney, Sydney, Australia.
authors.forename: Vanessa K
authors.initials: VK
authors.lastname: Morris
authors.forename: Margaret
authors.initials: M
authors.lastname: Sunde
mesh_terms: D020099:Coated Materials, Biocompatible / Q000737:chemistry; D004926:Escherichia coli; D005656:Fungal Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D057927:Hydrophobic and Hydrophilic Interactions; D055767:Immobilized Proteins / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry; D036103:Nanotechnology; D019906:Nuclear Magnetic Resonance, Biomolecular; D014176:Protein Biosynthesis; D058849:Protein Refolding; D013499:Surface Properties; D013501:Surface-Active Agents / Q000737:chemistry*; D017155:Wettability
chemical_list: D020099:Coated Materials, Biocompatible; D005656:Fungal Proteins; D055767:Immobilized Proteins; D013501:Surface-Active Agents