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/content/aip/journal/bmf/2/3/10.1063/1.2963104
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/content/aip/journal/bmf/2/3/10.1063/1.2963104
2008-07-10
2016-09-30

Abstract

90 kDa heat shock protein (HSP90) is a ubiquitous molecular chaperone and is one of the abundant proteins present in a cell under normal and stressed conditions. The adenosine triphosphate (ATP) binding region of HSP90 is currently under a great degree of study because of the interest of its role in cancer and protein maintenance; the binding of ATP to HSP90 induces a large conformational change in the protein as a result of the activity of different types of stressors within the cells. In the present paper, a simple microfluidicbiosensor is proposed for the characterization of ATP-HSP90 interactions through the principle of bioresistive variation. The experimental results prove that the present biosensor system is highly suitable for the detection of heat shock proteins present in a real-time biological sample, which is very useful for in-situ biomedical applications and rapid pathogenic detections.

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