2015 Volume 83 Issue 11 Pages 969-973
The HFBI protein, a type of hydrophobin, from Trichoderma reesei self-organizes in an orderly manner at either air/water or water/solid interfaces. The structural and electrochemical properties of self-organized membranes on different types of solid substrates (electrode materials) were investigated. Two types of substrates, highly oriented pyrolytic graphite (HOPG) and single crystal Au(111), were used for this study. Atomic force microscopy (AFM) showed that the self-organized HFBI membranes (prepared at the air/water interface) exhibited different structures on the two types of electrodes. In terms of the electrochemical results, both HFBI/HOPG and HFBI/Au(111) electrodes performed electrochemical reactions. Self-organized HFBI membranes did not provide insulation from electron transfer. Our findings that HFBI can be tagged with functional proteins, such as enzymes, by genetic fusion and utilized as a molecular carrier to fabricate molecular interfaces on an electrode.