Computational Strategies in Anticancer Drug Discovery: Virtual Screening of Protein Kinase Inhibitors

Abstract

Abstract Protein kinase CK2 is a crucial target for drug discovery due to its involvement in various cellular processes and diseases, including cancer. In this study, molecular docking and molecular dynamics (MD) simulations were employed to explore the binding interactions and stability of selected ligands with Zea mays CK2alpha (PDB ID: 4RLK). A library of 5000 compounds was screened using AutoDock Vina, followed by a refined docking analysis of the top 50 compounds with AutoDock. The molecular dynamics simulations, performed for 100 ns using the OPLS-2005 force field in Desmond, provided insights into the conformational stability of the protein-ligand complexes. Root Mean Square Deviation (RMSD), Root Mean Square Fluctuation (RMSF), and hydrogen bonding analyses revealed the structural stability and dynamic behavior of the ligands within the active site. The results highlight key interactions, including hydrogen bonding, π-stacking, and hydrophobic interactions, contributing to ligand binding and stability. These findings provide valuable insights into potential CK2alpha inhibitors and their role in drug design.