Exploration of the binding properties of the human serum albumin sites with neurology drugs by docking and molecular dynamics simulation

In this study, the binding properties of a set of neurology drugs to human serum albumin (HSA) were studied by docking and molecular dynamic (MD) methods. Based on the RMSD values for the MD simulation processes, the drug–protein complexes are stable. Site II of the HSA shows the best affinity for the studied drugs. Different kinds of interactions, including hydrogen bonding, π-cation interactions, and π–π interactions, are observable between ligand and protein during the MD simulation process. The MMGBSA calculations were done to evaluate the binding energy of the ligands and protein. The calculated energies are in good agreement with the previously reported experimental results. In some cases, there is a direct relation between the calculated binding energy with the half-life of the drugs, as it was expected.