Interaction of β-Lactoglobulin with Resveratrol: Molecular Docking and Molecular Dynamics Simulation Studies

In this work, the interaction of trans-resveratrol, as a natural polyphenolic compound, and Bovine β-lactoglobulin (BLG), was studied using molecular docking and molecular dynamics simulation methods. The molecular dynamics study makes an important contribution to understanding the effect of the binding of resveratrol on conformational changes of BLG and the stability of a protein-drug complex system in aqueous solution. Molecular docking studies revealed that the resveratrol was bound to the surface of the protein by two hydrogen bond interactions. The binding constant and free energy change, ΔG°, for the binding of resveratrol to BLG were about 6.6 × 105 mol L–1 and –33.4 kJ mol–1, respectively. Furthermore, the results of molecular dynamics simulation represented that the rmsd of unliganded BLG and BLG-resveratrol complex reached equilibration and oscillated around the average value after 600 ps simulation time. The study of the radius of gyration (Rg) revealed that BLG and BLG-resveratrol complexes were stabilized around 1500 ps and also exhibited no conformational change. Finally, analyzing the rms fluctuations suggested that the structure of the ligand binding site remains approximately rigid during the simulation.