Binding of NDGA and morin with phospholipase A2: experimental and computational evidences

Abstract

The effects of morin and nordihydroguaiaretic acid (NDGA), two plant secondary metabolites, on porcine pancreatic phospholipase A2 (PLA2) were investigated by isothermal titration calorimetry (ITC) and in silico docking analyses. The binding energies obtained for NDGA and morin from the ITC studies are − 6.36 and − 5.91 kcal mol− 1, respectively. Similarly, the glide scores obtained for NDGA and morin towards PLA2 were − 7.32 and − 7.23 kcal mol− 1, respectively. Further the docked complexes were subjected to MD simulation in the presence of explicit water molecules to check the binding stability of the ligands in the active site of PLA2. The bound ligands make hydrogen bonds with the active site residues of the enzyme and coordinate bonds with catalytically important Ca2+ ion. The binding of ligands at the active site of PLA2 may also contribute to the reported anti-inflammatory properties of NDGA and morin.