Assessment of Nutritional Status of Children aged 1-5 years attending the Outdoor Patients Department of Sheikh Zayed Hospital, Rahim Yar Khan, Pakistan

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: In Silico study (Computational modeling). Place of Study: International Center of Medical Sciences Research (ICMSR), Islamabad, Pakistan. Material and Methods: Using the Swiss PDB Viewer, the structural features of CYP1A2 were assessed, focusing on key residues, motifs, helices, and conserved regions. Results: Our findings identified specific binding sites for Alpha-Naphthoflavone (ANF), highlighting its potential as a potent inhibitor of CYP1A2. This research contributes to our knowledge of the clinical and toxicological implications associated with CYP1A2. Conclusion: Structural differences were found between CYP1A2 and related enzymes, with less than 40% sequence identity compared to several other P450s. The study predominantly compares CYP1A2 with CYP 2A6 and CYP3A4 due to these differences. T he developed structural models offer a fast and precise method for studying CYP1A2, aiding in understanding its role in drug metabolism and toxicology.