The Effect of Hydrophobin Protein on Conductive Properties of Carbon Nanotube Field-Effect Transistors: First Study on Sensing Mechanism.

Abstract

Hydrophobin is a surface active protein having both hydrophobic and hydrophilic functional domains which has previously been used for functionalization and solubilization of graphene and carbon nanotubes. In this work, field-effect transistors based on single nanotubes have been employed for electronic detection of hydrophobin protein in phosphate buffer solution. Individual nanotubes, single- and multiwalled, are characterized by atomic force microscopy after being immersed in protein solution, showing a relatively dense coverage with hydrophobin. We have studied aspects such as nanotube length (0.3-1.2 µm) and the hysteresis effect in the gate voltage dependent conduction. When measured in ambient condition after the exposure to hydrophobin, the resistance increase has a strong dependence on the nanotube length, which we ascribe to mobility degradation and localization effects. The change could be exceptionally large when measured in-situ in solution and at suitable gate voltage conditions, which is shown to relate to the different mechanism behind the hysteresis effect.