Original scientific paper
Interaction of β-Lactoglobulin with Resveratrol: Molecular Docking and Molecular Dynamics Simulation Studies
M. Sahihi
; Department of Chemistry, University of Isfahan, Iran
Y. Ghayeb
; Department of Chemistry, Isfahan University of Technology, Iran
A. Khalegh Bordbar
; Department of Chemistry, University of Isfahan, Iran
Abstract
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.
Keywords
Bovine beta lactoglobulin; resveratrol; molecular docking; binding; molecular dynamics simulation
Hrčak ID:
112351
URI
Publication date:
19.12.2013.
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