Molecular Docking of Some quinazolinone Analogues as an EGFR Inhibitors

Rafian boroujeni, Mahdi and Rezaeinasab*, Rezvan (2021) Molecular Docking of Some quinazolinone Analogues as an EGFR Inhibitors. Yafteh, 23 (3).

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Abstract

Background: Mutations that cause high expression of epidermal growth factor can lead to cancer. Hence, this factor serves as a potential molecular target for cancer treatment, and inhibitors of this enzyme are of particular importance in the treatment of cancer. The aim of this study is to investigate the bioinformatics of inhibition of EGFR enzyme by a number of quinazolinone derivatives. Materials and Methods: This research was done by descriptive-analytical method. To investigate how quinazolinone derivatives bind to the active site of the enzyme, the chemical structure of the compounds was first plotted using ChemBioDrawUltra software version 14. It was then transferred to Hyperchem software for energy optimization. Docking studies were performed using AutoDock 4.2 software and in the final stage, the results were analyzed using three programs: AutoDockTools, DS Visualizer and Ligplot. Results: Based on the results of docking studies, the most important bonds involved in drug-receptor binding are hydrophobic bonds and hydrogen bonds. Among all the studied compounds, the best docking results are related to compound number 3. This compound with the most negative binding energy level (ΔGbind =-7.53 Kcal / mol) has a greater tendency to bind to key amino acids at the active site of the EGFR. Conclusion: In the end, due to the high effectiveness and docking results, it can be conclude that compound number 3 can be considered as an effective erlotinib EGFR inhibitor. Keywords: Bioinformatic, Molecular docking, quinazolinone, EGFR.

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