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Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins
Sarah R Ball1, Chi L L Pham1, Victor Lo1
1Discipline of Pharmacology and Sydney Nano, University of Sydney, Sydney, NSW, Australia.
Abstract:
The fungal hydrophobins are small proteins that are able to self-assemble spontaneously 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 the protocols for the production and purification of recombinant hydrophobins and oxidative refolding to a biologically active, soluble, monomeric form. We describe methods to trigger the self-assembly into the fibrillar rodlet state and techniques to characterize the physicochemical properties of the polymeric forms.
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