Multi-spectral techniques and molecular docking to investigation of the interaction between ferulic acid and pepsin

Abstract

In this work, the interaction between ferulic acid (FA) and pepsin was explored by UV–visible absorption spectroscopy, fluorescence spectroscopy, synchronous fluorescence, circular dichroism (CD) spectroscopy, Fourier transform infrared spectroscopy (FT-IR) and molecular docking. The results of fluorescence revealed that FA had a strong ability to quench the intrinsic fluorescence of pepsin through a static quenching procedure. The binding constant and the number of binding sites were determined. Thermodynamic dates and docking information suggest that FA combine with pepsin is mainly driven via electrostatic force. It also requires synergistic drive of hydrophobic and hydrogen bonding. The consequences from UV–Vis, synchronous, CD and FT–IR spectra measurements manifested that the secondary structure of pepsin was changed and the microenvironments of certain amino acid residues was modulated by the binding of FA. FA induced conformational changes in pepsin. The β-sheet, α-Helix, and Random fractions of pepsin increased and the β-turn decreased with the treatment of FA. In addition, analysis of pepsin activity assay measurements confirmed that FA reduced enzymatic activity of pepsin within the investigated concentrations. This work studied the inhibitory effects and revealed mechanisms of the interaction between FA and pepsin in vitro, and suggested that FA could be a potential component to affect the structure and properties of digestive enzyme.