Assembling of redox proteins on Au(111) surfaces: A scanning probe microscopy investigation for application in bio-nanodevices

The morphology and conductive properties of azurin molecules, chemically attached to sulfhydryl terminated alkanethiol monolayer assembled on Au(111) surface, are mapped at single molecule level and compared with those observed for the same molecule immobilised on bare Au(111). High-resolution Tapping Mode Atomic Force Microscopy shows that the protein molecules immobilised on modified gold, better reproduces the crystallographic height of the protein, than that immobilised on bare gold. Such a height recovering is also found in the Scanning Tunnelling Microscopy images. Consistently, a good tunnelling conduction of azurins on the modified gold electrode is demonstrated by Tunnelling Spectroscopy. Cyclic voltammetry measurements show, in addition, that the redox activity of azurin molecules covalently immobilised on sulfhydryl functionalised Au(111) surface is retained. These results are discussed in connection with possible use of this linker in the assembling of nano-hybrid systems.