A Computational Study on the Blocking Ability of Selected Commercially Available Anticancer Drugs and Their...

Computational studies were done on the complexes between some commercially available anticancer drugs and their hypothetic derivatives and the CCR5 protein. At first step, the docking studies were done to obtain the best ligand that can inhibit the CCR5 protein. Based on the binding energy results obtained from the docking studies, 16 complexes were selected. Molecular dynamic studies were carried out on these structures and then molecular mechanics-generalized Born surface area calculations were done to find the binding energies of the ligands to the CCR5 protein. Based on the investigation of the binding modes of the ligands to the CCR5 protein, the TYR and ALA have more tendency to bind to the ligand moieties. By decomposing of the binding energies, it was found that the van der Waals interactions have the most important role in the binding of ligands to the protein in comparison with the electrostatic and hydrogen bonding interactions. The results of the interaction potential surface map analysis showed that the nitrogen and oxygen atoms have a relatively similar role in the binding of ligands to the CCR5 protein structure.