1 research outputs found
Kinetics and Control of Self-Assembly of ABH1 Hydrophobin from the Edible White Button Mushroom
Hydrophobins are small fungal proteins
that self-assemble at hydrophobic/hydrophilic
interfaces to form stable, amyloid membranes that are resistant to
denaturation. Their remarkable surface activity has driven intense
research for their potential utility in biomedical and cosmetic applications.
In this research, the self-assembly characteristics of the Class I
hydrophobin ABH1 from Agaricus bisporus, the edible white button mushroom, were evaluated as a function
of solution and interface properties, in an attempt to gain greater
mechanistic understanding. The kinetics of self-assembly were examined
using dynamic quartz crystal microbalance techniques in combination
with AFM, ellipsometry, contact angle goniometry, light scattering,
and circular dichroism spectroscopy. It was found that the strength
of interfacial tension between two phases drives the speed of ABH1
assembly and that the nature and location of the molecular ordering
was influenced by temperature. ABH1 demonstrates different characteristics
and self-assembly properties than those reported for other Class I
hydrophobins, including causing an instantaneous decrease in surface
tension in aqueous solution and undergoing a direct transition to
β-sheet conformation on self-assembly at elevated temperature