Hydrophobins are amphipathic proteins produced by filamentous fungi that moderate interfacial processes through the formation of stable amyloid membranes. Hydrophobins isolated in the laboratory self-assemble at hydrophobic/hydrophilic interfaces, and assembled structures bind tightly to organic and inorganic substrates. Self-assembly and adsorption characteristics of the class two ABH1 hydrophobin isolated from Agaricus bisporus(the white button mushroom) were examined as a function of substrate and solution environment via quartz crystal microscopy, atomic force microscopy and circular dichroism spectroscopy. Factors influencing the self-assembly process were elucidated, which could prove useful in controlling the behavior of hydrophobins for specific applications.

Self-assembly processes of ABH1 hydrophobin protein

246th National Meeting (2013)

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