XVI International Botanical Congess

The SC3 hydrophobin protein from Schizophyllum commune self-assembles in an aqueous environment to form vesicles with hydrophobic interior and hydrophilic exterior surfaces. We are studying the protein's ability to entrap a hydrophobic material from an aqueous environment in vesicles and the mechanism by which this occurs. Utilizing a radiolabeled 14C-hexadecane sequestration assay, we are able to quantify the amount of hydrophobic material that can be removed from an aqueous environment by hydrophobin. Epifluorescent microscopy studies using Nile Red and calcein demonstrate that hydrophobin vesicles entrap hydrophobic molecules within the vesicle interior. Insight into the mechanism of hydrophobin protein self-assembly can be determined using fluorescence spectroscopy.