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.
CITATION STYLE
Ball, S. R., Pham, C. L. L., Lo, V., Morris, V. K., Kwan, A. H., & Sunde, M. (2020). Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins. In Methods in Molecular Biology (Vol. 2073, pp. 55–72). Humana Press Inc. https://doi.org/10.1007/978-1-4939-9869-2_4
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