Bioresistive identification of heat shock protein 90.
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 microfluidic biosensor 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.
Chandrasekaran
Arvind
A
Pakkiriswami
Shanmugasundaram
S
You
Jian Liang
JL
Acharya
Ashwin
A
Packirisamy
Muthukumaran
M
Maxwell
Denis
D
Annu Rev Biochem. 2006;75:271-94
16756493
J Biochem. 2005 Apr;137(4):443-7
15858167
Cancer Lett. 2004 Apr 8;206(2):149-57
15013520
Sensors (Basel). 2007 Sep 11;7(9):1901-1915
28903204
Science. 2000 Apr 14;288(5464):316-8
10764640
Mol Cancer Ther. 2004 Aug;3(8):1021-30
15299085
Nihon Yakurigaku Zasshi. 2003 Jan;121(1):33-42
12617036