Molecular modeling studies on the binding of Gallic acid to human serum albumin

In this study, the interaction of gallic acid as an anticancer compound with human serum albumin(HSA) was investigated by molecular docking simulation. Binding free energy(ΔG), electrostatic interactions(Eelec) and van der waals energies(Evdw) between Gallic acid and HSA were calculated on the basis of force field energy calculations. From the docking simulation the magnitudes of ΔG, Eelec and Evdw of gallic acid binding with HSA for the site Ι (subdomain ΙΙA) were obtained -4.89, -4.47, -1.91, and for site ΙΙ (subdomain ΙΙΙA) they were calculated to be -3.89, -4.17 and -0.7 kcal mol-1, respectively. The results indicated that gallic acid could bind to the site Ι more stronger than site II of HSA mainly by hydrophobic interaction.

Keywords:

HSA , Gallic Acid , Molecular docking