Docking studies with the CYP2E1 active site and pyrazole derivatives

CHED 1292

Daniel Judkins, jud42093@obu.edu1, 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 4307, Arkadelphia, AR 71998, (2) Department of Biochemistry & Molecular Biology, University of Arkansas for Medical Sciences, 4301 W. Markham, Little Rock, AR 72205
The enzyme CYP2E1 has the capability to oxidize more than 70 small, hydrophobic chemicals. Because CYP2E1 recognizes such a diverse class of substrates, it is difficult to interpret and predict enzymatic reactions. In theory the CYP2E1 enzyme possesses a restrictive active site capable of binding either a single two-ringed or two single-ringed molecules. Previous docking studies have determined that molecules will either bind to a proximal or distal site relative to the heme. To continue with the idea of the restrictive active site in CYP2E1, pyrazole derivatives have been docked using the Surflex module in Sybyl7.2. Results illustrated that binding occurs in either the effector or distal site. The studies provide a better understanding of how ligands interact with the two binding sites in CYP2E1.
 

Undergraduate Research Poster Session: Medicinal Chemistry
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Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008