Predicting binding interactions of ring substrates with CYP2E1 using homology modeling

CHED 1343

Ryan M. Laddusaw, lad38593@obu.edu1, Martin D. Perry Jr., perrym@obu.edu1, and Grover Paul Miller2. (1) Department of Chemistry, Ouachita Baptist University, 410 Ouachita Street, Box 3711, Arkadelphia, AR 71998, (2) Department of Biochemistry & Molecular Biology, University of Arkansas for Medical Sciences, 4301 W. Markham, Little Rock, AR 72205
Cytochrome P450 2E1 (CYP2E1) is a biologically important protein that metabolizes many small hydrophobic compounds. Using computer modeling, the binding orientation of one and two ringed substrates can be determined and the metabolized product can be predicted. In conjunction with theses studies, the docking of multiple substrates and inhibitors will be compared to kinetic studies to determine the accuracy of the homology model.
 

Undergraduate Research Poster Session: Medicinal
2:00 PM-4:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster

Division of Chemical Education

The 233rd ACS National Meeting, Chicago, IL, March 25-29, 2007