Abstract
Background: Cytochrome P450 enzymes play vital roles in metabolizing drugs, endogenous compounds, and environmental pollutants. Among them, Cytochrome P450 1A2 (CYP1A2) CYP1A1 and CYP1B are particularly important for activating carcinogens. Computational modeling of CYP1A2 is essential for understanding its interactions with various molecules, substrates, and inhibitors. Objective: To characterize the structure of CYP1A2 and explore the binding of alpha-naphthoflavone to its active site. Study design: Computational modelling??? Place and duration of study: ----------------- Material and Methods: Using the Swiss PDB Viewer, we assessed the structural features of CYP1A2, focusing on key residues, motifs, helices, and conserved regions. Results: Our findings identified specific binding sites for alpha-naphthoflavone, highlighting its potential as a potent inhibitor of CYP1A2. This research contributes to our knowledge of the clinical and toxicological implications associated with CYP1A2. Keywords: Alpha-naphthoflavone Cytochrome P450, CYP1A2, Computational modeling, Structural characterization.
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