Study of Interaction of Human Serum Albumin with Doxorubicin (Anti-Cancer Drug) by Docking Simulation

Human serum albumin (HSA) is one of the main endogenous vehicles for biodistribution of molecules by blood plasma. Association constants and thermodynamic parameters for the interaction of HSA with doxorubicin were studied by docking. Docking study suggests that doxorubicin is able to interact with HSA by means of hydrogen bond with one arginine residue, whereas the hydroxyl group is inserted in a hydrophobic pocket. The estimated of Gibbs free energies (ΔG°) is equal to -9.1 kcal/mol for the best model. The negative values of ΔG° indicate a spontaneous process. The association constant value (Ka ≈ 8×103 L.mol−1) is favorable for its efficient biodistribution by blood plasma.