Putative Binding Sites of Dopamine and Arachidonoyl Dopamine to Beta-lactoglobulin: A Molecular Docking and Molecular Dynamics Study

Because of participation in many aspects of human life, and due to oxidation-sensitive characteristics of dopamine (DA) and arachidonoyl dopamine (AA-DA), the necessity of biocompatible carrier to keep them against oxidation is of importance. In this work, we explored the putative binding sites of DA and AA-DA to -lactoglobulin (BLG) as potent carrier. Docking results identified the binding sites, involved residues and driving forces to the binding process of these ligands. The dissimilar binding site of AA-DA in comparison with DA has been designated by different values of Gibbs free energy, biding constants and contact residues. Molecular dynamics simulation outcomes confirmed that both compounds stayed in their predicted binding sites during the entire time of simulation with no major secondary and tertiary protein structural changes which pointed that BLG might be considered as a suitable oxidation-protective carrier for these compounds.