CYP2E1, a member of the cytochrome P450 super family of monooxidases, has been shown to metabolize a variety of small, nonpolar, cyclical compounds. The drug design and administration community are particularly interested in cytochrome P450s for their ability to metabolize drugs into inactive or carcinogenic forms. CYP2E1 is of special interest for its novel substrate inhibition kinetics of unknown physiological implications. To investigate both CYP2E1's substrate inhibition and metabolic mechanism, a series of computational tests involving a combination of Surflex-Dock and molecular dynamics on a Sybyl X 1.3 mac platform are used. Docking is simulated with an array of pyrazole inhibitors. Through this study, residues of interest for both single and multiple docked ligands are designated. In particular, LEU210 has been associated as a functional residue for stable docking of a second ligand in the 'effector' site within the channel and substrate inhibition.

Computational docking of pyrazole derivatives into CYP2E1

245th National Meeting (2013)

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