Hydrophobins are amphipathic, fungal proteins which have the ability to self-assemble at hydrophobic/hydrophilic interfaces, altering interfacial properties by creating an amphipathic, intermediary layer.  In this research, the hydrophobin ABH1 (from the edible white button mushroom) was studied to explore the characteristics of hydrophobin self-assembly into beta-sheets. Protein structure and film formation were studied at the air/water interface, at the water/substrate interface and in the bulk of solution. Surface tensiometry results supported previous reports of rapid self-assembly at the air/water interface. Circular dichroism data suggest that assembly occurs in the bulk of solution only at elevated temperatures. Quartz crystal microbalance results indicate that hydrophobic surfaces such as polystyrene promote quicker adsorption than do hydrophilic surfaces such as silicon oxide.  Knowledge of the assembly mechanisms of hydrophobins will enable further investigation into potential applications.

Insight into the mechanism and kinetics of self-assembly of the hydrophobin protein ABH1

243rd National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.