Molecular docking approach on the molecular interactions involving beta-lactoglobulin (βLG)-4-Dicyanomethylene2,6-Dimethyl-4-Hpyran (DDP) dye in the presence of an antibiotic, norfloxacin

Abstract

Molecular docking (MD) techniques were employed in the determination of binding stability of Beta-lactoglobulin (βLG) with 4-Dicyanomethylene2,6-Dimethyl-4-Hpyran (DDP) dye in the presence of quinolone-based antibiotic, norfloxacin (NOR). βLG acts as the host and drug/dye is employed as the guest molecule. The energetics and molecular interaction parameters of βLG-DDP were found to be stable than βLG-NOR. DDP resides in three distinguishably different binding sites of βLG, however the binding energies does not differ considerably. Interestingly, the energetics of βLG-NOR conformers differs significantly and reveals the existence of two distinguishable conformers. NOR acts as a hydrogen-bonding (HB) acceptor and the amino acid (AA) residues of βLG as the donor. The extent of HB interactions predominates over hydrophobic interactions in βLG-NOR than βLG-DDP complex. MD studies authenticates no direct binding of dye-drug inside the domains of βLG, when docked simultaneously. On the contrary, docking of dye to βLG-NOR complex enhances the binding stability. Several molecular interactions govern the stability of the complex and play a major role on the binding affinity of the host-guest complex in the presence of two competitive ligands. MD techniques authenticate that DDP/NOR is bound to several AA residues through conventional and non-conventional HB interactions accompanied with hydrophobic, pi-pi, pi-alkyl and van der Waals forces of interactions. Further, MD methods is employed as an efficient tool and a non-evasive technique in establishing the stability of 1:1complex of drug/dye with βLG in the present study.