Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins

Sarah R Ball; Chi L L Pham; Victor Lo; Vanessa K Morris; Ann H Kwan; Margaret Sunde

doi:10.1007/978-1-4939-9869-2_4

Formation of Amphipathic Amyloid Monolayers from Fungal Hydrophobin Proteins

Methods Mol Biol. 2020:2073:55-72. doi: 10.1007/978-1-4939-9869-2_4.

Authors

Sarah R Ball¹, Chi L L Pham¹, Victor Lo¹, Vanessa K Morris², Ann H Kwan³, Margaret Sunde⁴

Affiliations

¹ Discipline of Pharmacology and Sydney Nano, University of Sydney, Sydney, NSW, Australia.
² School of Biological Science, University of Canterbury, Canterbury, New Zealand.
³ School of Life and Environmental Sciences and Sydney Nano, The University of Sydney, Sydney, NSW, Australia.
⁴ Discipline of Pharmacology and Sydney Nano, University of Sydney, Sydney, NSW, Australia. margaret.sunde@sydney.edu.au.

PMID: 31612436
DOI: 10.1007/978-1-4939-9869-2_4

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.

Keywords: Amphipathic monolayer; Functional amyloid; Hydrophobins; Rodlet; Self-assembly.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Fungal Proteins / chemistry*
Hydrophobic and Hydrophilic Interactions
Nanostructures / chemistry

Substances

Fungal Proteins