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.
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Acknowledgements
The authors would like to thank Dr. Ann Kwan for development of the recombinant expression and oxidative refolding protocol and for her advice and assistance. This work was supported by funding from the National Health and Medical Research Council of Australia (CDA402831) and the Australian Research Council (LP0776672 and DP0879121).
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Morris, V.K., Sunde, M. (2013). Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins. In: Gerrard, J. (eds) Protein Nanotechnology. Methods in Molecular Biology, vol 996. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-354-1_7
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DOI: https://doi.org/10.1007/978-1-62703-354-1_7
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Publisher Name: Humana Press, Totowa, NJ
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