Interaction Of Imatinib With 2ghw(Sars-Cov2 Spike) Protein Structure: A Molecular Docking Study

Abstract

The goal of this work is to check how strong the interaction is between Imatinib and the 2GHW protein structure and whether or not it has any potential inhibition. Imatinib’s potential as a tyrosine kinase inhibitor is examined in this context with respect to the 2GHW protein, which is relevant to known signaling pathways. AutoDock Vina was utilized for docking simulations and the results have estimated the binding free energy to be -7.34 kcal/mol and the inhibition constant to be 4.20 µM, while the temperature was fixed at 298.15 K. Among the key interactions formed are van der Waals forces, hydrogen bonds and electrostatic interactions. Intermolecular energy of -9.42 kcal/mol had acceptable binding energy to these molecules. Based on the data listed this type of molecular docking study offers possibilities for understanding the molecular mechanisms of Imatinib action at the level of 2GHW protein structure. This will assist in designing additional inhibitors of these and similar proteins in disease situation