High-frequency impedance biosensors with nanometer gaps have been prepared for the detection of biomolecular interactions such as protein-antibody and protein-aptamer binding. The sensor principle is based on electrical impedance changes measured at 1.2 GHz due to changes of the effective dielectric constant within the 68 nm gaps between two gold electrodes. As a model system, the specific binding of the blood clotting factor human thrombin with different concentrations to its ribonucleic acid (RNA) α-thrombin aptamer, as well as the immobilization process of the RNA-aptamer, have been detected in real time. By using a similar 68 nm-gap sensor blocked with bovine serum albumin and a reference sensor with 10μm electrode spacing, signal changes due to variations of the bulk dielectric constant due to buffer/analyte solutions, and unspecific binding events have been analyzed.
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Löhndorf et al. (2005) studied this question.
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