Electrochemical characterization of BSA/11-mercaptoundecanoic acid on Au electrode

Recently, it has becoming increasingly important to control the organization of self-assembled monolayers (SAMs) of functionalized thiols and to bind various proteins on gold/silicon substrates for their potential integration in nanoscale sensors/biosensors and optical devices. The biomolecule immobilization on the surfaces by covalent chemistry allows fabrication of reproducible, protein-modified surfaces and became also a model to investigate the electrochemical response induced by protein binding. In this study, we report different nanostructured gold substrates and the adsorption of a protein, bovine serum albumin (BSA) on the 11-mercaptoundecanoic acid (MUA) layer for further biomedical applications. Nanostructured gold layers of 200 nm thickness have been prepared on both, flat and macroporous silicon (macroPS) substrates. The X-ray diffraction analyses emphasized a dominant (1 1 1) crystallographic orientation of nanostructured Au substrates, which is preferred orientation for binding and detection of organic molecules on the gold surface. Impedance spectroscopy measurements performed in specific frequency ranges show that the binding of protein to a single monolayer of MUA can be easily detected. The impedance changes were also corroborated with cyclic voltammetry and Raman spectroscopy analysis for further development of the biosensor transducer for converting of the specific molecular recognition events into either an optical or electrical signal.