Tuning molecular orientation in protein films

• Published in: Surface science Vol. 542; no. 1; pp. 64 - 71
• Main Authors: Alessandrini, Andrea, Gerunda, Mimmo, Facci, Paolo, Schnyder, Bernhard, Kötz, Rüdiger
• Format: Journal Article
• Language: English
• Published: Lausanne Elsevier B.V 10.09.2003; Amsterdam Elsevier Science; New York, NY
• Subjects: Atomic force microscopy; Biological and medical sciences; Biological molecules – proteins; Condensed matter: structure, mechanical and thermal properties; Electrochemical methods; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Molecular biophysics; Physics; Solid-fluid interfaces; Surface properties. Adsorption; Surfaces and interfaces; thin films and whiskers (structure and nonelectronic properties); Wetting; Atomic force microscopy; Electrochemical methods; Biological molecules – proteins; Biomolecular electronics; Cyclic voltammetry; Liquid solid interface; proteins; Atomic force microscopy; Electrochemical methods; Molecular orientation; Spectroscopic ellipsometry; Monolayers; Experimental study; Metalloproteins; Photoelectron spectroscopy; Biological molecules
• ISSN: 0039-6028; 1879-2758
• DOI: 10.1016/S0039-6028(03)00922-1

The rational design of azurin metalloprotein assemblies suitable for biomolecular electronics application has been achieved by exploiting different surface chemical approaches for growing active protein layers on both metal and insulating surfaces. The formed layers, which have been tested extensively by scanning force microscopy (SFM), spectroscopic ellipsometry, X-ray photoelectron spectroscopy (XPS), and electrochemical measurements (cyclic and linear voltammetry (CV and LV)), consist of redox active molecules endowed with tuneable orientation according to the particular functional group exploited for surface immobilization. The peculiar molecular arrangement has turned out to be responsible for different transport properties in solid state hybrid electronic planar devices.