There are many biological macro-molecules such as nucleic acids, lipids, carbohydrates and proteins. While each of them plays a vital (and interesting) part in life but there is something special about the proteins. Proteins are the key link between the processes of information and replication that take place on a genetic level and the infrastructure of living features. Understanding the properties of proteins is the key to understanding the spark of the life. In this paper we describe our study of various electrical properties of protein when performing measurements at the nanoscale. To achieve this goal we designed and fabricated a nanoelectronic probe. This nano structure consists of four thin film layers. There are two conductive layers and an insulative layer in between. There is also a protective oxide layer as the top most layer. This layer is to prevent the exposure of conductive electrodes to the solution. Underneath the bottom electrode, there is another oxide layer, which can be a thermally grown oxide. This layer insulates the first electrode from the substrate. In this study, while we use non-specific detection of streptavidin protein as a proof of concept, we emphasize that the findings of this study can be extended to specific detection of target proteins, where in this case a specific probe molecule would also be immobilized on the sensor surface.

Here we present the development of an array of electrical nano-biosensors in a microfluidic channel, called Nanoneedle biosensors. Then we present the proof of concept study for protein detection. A Nanoneedle biosensor is a real-time, label-free, direct electrical detection platform, which is capable of high sensitivity detection, measuring the change in ionic current and impedance modulation, due to the presence or reaction of biomolecules such as proteins or nucleic acids. We show that the sensors which have been fabricated and characterized for the protein detection. We have functionalized Nanoneedle biosensors with receptors specific to a target protein using physical adsorption for immobilization. We have used biotinylated bovine serum albumin as the receptor and sterptavidin as the target analyte. The detection of streptavidin binding to the receptor protein is also presented.