Molecular Interactions between a Flavonoid and Lysozyme: A Spectroscopic, Thermodynamic, and Computational Study

Abstract

AbstractTransferulic acid has therapeutic importance hence it is very crucial to understand how this molecule interacts with lysozyme proteins for the purpose of drug design, and evaluation. The study is very helpful for drug pharmacology and the thermodynamic parameters of the polyphenolic compound and this protein interaction which is important for disease encounter and prevention. Here the spectroscopic, thermodynamic, and computational study has been reported as experiments. The CD study of the binding of lysozyme and trans ferulic acid found significant structural stability of the protein. Spectroscopically the UV‐Vis & fluorescence study has shown a substantial shift of absorption spectra in the binding of these two molecules, to confirm the interaction. An ITC experimental study found an affinity of the molecule to protein with a binding constant of Ka having a significant value. The Molecular Dynamics study found details of the geometric posture and main force of binding of TFA molecule upon binding with lysozyme site in PBS buffer at physiological pH value. The complex of lysozyme and trans ferulic acid also proved as a stable conformation by Molecular Dynamics study. In the DSC study, stable interaction of lysozyme and trans ferulic acid is shown upon changing the melting enthalpies and temperatures.