Interaction mechanism between resveratrol and ovalbumin based on fluorescence spectroscopy and molecular dynamic simulation

Proteins act as excellent biological carriers for resveratrol (RES) delivery. However, the interaction between RES and proteins remains unclear. In this work, ovalbumin (OVA) was selected as a protein model based on fluorescence spectroscopy and molecular dynamic (MD) simulation to investigate the interaction mechanism between RES and OVA. Fluorescence spectroscopy coupled with the Stern-Volmer equation verified the static fluorescence quenching types of RES and OVA. The static quenching binding affinity is 1.41 & times; 104 L/mol. The number of stoichiometric binding values with approximately 1.0 indicates that one RES molecule could bind to only one OVA molecule. The simultaneous fluorescence and three-dimensional fluorescence spectra of the interaction between RES and OVA demonstrated the altered conformation and microenvironment of OVA. The microenvironment formed by tryptophan or tyrosine residues increased polarity and weakened hydrophobicity. Through MD simulation techniques, hydrogen bonds and hydrophobic interactions promoted RES-OVA complexation. MD results showed that RES likely interacted with OVA residues ALA-326, GLN-325, SER-165, GLN-162, LEU-161, LYS-290, TYR-291, and LEU-293. RES and OVA formed a more stable complex because of various forces. Therefore, studying the interaction of RES and OVA helps expand the potential applications of OVA as a RES delivery system.

Automated summary

Proteins, especially ovalbumin, can serve as effective carriers for delivering resveratrol. Through fluorescence spectroscopy and molecular dynamic simulation, the interaction mechanism between resveratrol and ovalbumin was investigated, revealing static fluorescence quenching, binding affinity, microenvironment changes, and specific residues involved in the interaction. The study highlights the potential of ovalbumin as a resveratrol delivery system.