Conformational detection of heat shock protein through bio-interactions with microstructures

Abstract

The molecular mechanical interaction between the heat shock protein 90 (HSP90) and the adenosine triphosphate (ATP) molecules is detected by employing a polyvinyl-di-chlorofluoride (PVDF) aluminum-coated microcantilever beams, considered as a mechanical transducer. Here the chaperone protein called HSP90 performs the interaction. The microcantilever beam will sense the molecular mechanical interaction between the HSP90 and ATP molecules. This protein forms a complex molecule with ATP, and because of this molecular interaction, the beam will deflect which is measured using the optical lever method. This optical technique is able to detect the biomechanical interaction of ATP and HSP90 at various concentrations. The response time and sensitivity of this technique are found to be superior to similar methods such as piezoresistive technology known to be used for studying biomolecules interaction. This work will enable the reader to understand the behavior of micro-electro-mechanical systems (MEMS) based microcantilever structure under the influence of different concentrations of HSP90. The work provides a methodological approach to develop point-of-care devices for the detection of biomolecules.