Calorimetric, spectroscopic and computational investigation of morin binding effect on bovine serum albumin stability

Abstract The interaction of morin (Mor) with bovine serum albumin (BSA) was investigated using calorimetric, spectroscopic and computational methods. The ligand binding to protein has been studied under physiological conditions at various temperatures using isothermal titration calorimetry (ITC). Furthermore, the enthalpy (ΔH), entropy (ΔS) and heat capacity (ΔCp) changes of ligand-protein complex formation were also calculated. The results indicated two sites for Mor binding with BSA. The presence of Mor in higher concentration caused an increased thermal stability of protein proved by differential scanning calorimetry (DSC) measurements. Molecular docking and dynamics simulations supported Sudlow’s sites I and II of BSA as binding receptors for Mor. The dual action of ligand binding was demonstrated: stabilizer of the native protein structure up to the denaturation temperature and promoter of aggregation above this temperature.