Investigation Of In-Silico Studies Of Cytochrome P450 Inhibitors

Abstract

The current paper describes computational techniques for designing the three-dimensional structure of the human enzyme "Cytochrome P450 4A11" using the Uniprot sequence (UniProtKB – Q02928). To create a three-dimensional model of the cytochrome P450 protein, a homology modelling study was conducted. The Modeler9.17 software application was used to create the model. The AUTODOCK4.2 program was used to further dock the generated model with medications that were already on the market. Molecular docking tests were conducted using Autodock4.2 with four medicines after the model was designed in order to determine the functional effect of the protein. Over 89% of the amino acids in the most preferred region are displayed in the created model. Every medication exhibits strong interactions and binding energy. When interacting with Gly453, the molecule telenzepine exhibits the greatest binding energy of -9.69 kCal/mol. various studies offer insight and interpretation into the data generated by various techniques. It clarifies how molecules interact in the area of the active site.