Development of "smart” biofilters based on the ligand binding protein Calmodulin

ANYL 159

Santoshkumar Khatwani, santoshkhatwani@yahoo.com, Jonathan Morris, jonjon2k2@hotmail.com, Elissavet Moschou, l_moschou@yahoo.com, Nitin Chopra, nchop2@gmail.com, Leonidas Bachas, bachas@uky.edu, and Sylvia Daunert, daunert@uky.edu. Department of Chemistry, University of Kentucky, Rose street, Chem-phys building, University of Kentucky, Lexington, KY 40506
The developed smart biofilters are based on polymeric membranes with specific porosity on which ligand binding proteins have been immobilized. The binding proteins undergo conformational changes upon binding to their ligands. These protein conformational changes can obstruct or expose the pores of the membrane, thus altering selectively the flow rate of the test solution across the membrane, in the presence of a target analyte. The protein Calmodulin, which is selective to the class of anti-depressant drugs phenothiazines, has been utilized as the model protein. It is demonstrated that the flow rates of these membranes are significantly increased in the presence of the phenothiazine, chlorpromazine. These changes are reversible, depending on the presence or absence of the target analyte in solution. Smart biofilters are low-cost and simple to fabricate and use. This strategy is suitable for the development of filtration systems and biosensors that can be utilized in field analysis.
 

General Papers
7:00 PM-9:00 PM, Sunday, 10 September 2006 Moscone Center -- Hall D, Poster

Division of Analytical Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006