Study on the interaction mechanism of virgin olive oil polyphenols with mucin and α-amylase

The interaction mechanism of mucin and alpha-amylase with virgin olive oil (VOO) polyphenols (oleuropein (OL), tyrosol (TY), hydroxytyrosol (HT)) was analyzed by fluorescence, ultraviolet (UV) absorption, attenuated total reflection Fourier transform infrared (ATR-FTIR), circular dichroic (CD) spectroscopy and molecular docking. A total of 17 polyphenols have been identified in the selected VOO, and the TY, HT and OL were the main compounds. The quenching mechanism between mucin/alpha-amylase and three VOO polyphenols was static, mainly through van der Waals forces and hydrogen bonds. The results of UV absorption, ATR-FTIR, and CD spectroscopy revealed that the conformation of mucin changed after combining with the three polyphenols, while that of the alpha-amylase changed little. Molecular docking predicted the interaction sites of the three polyphenols with human salivary mucin and alpha-amylase. The present study could provide the theoretical foundation for further research on the interaction between human salivary protein and phenolic compounds in VOO.

Automated summary

This study investigated the interaction mechanism of mucin and alpha-amylase with polyphenols in virgin olive oil through various spectroscopic methods and molecular docking, revealing a static quenching mechanism and conformational changes in mucin. Molecular docking also predicted the binding sites of polyphenols with human salivary mucin and alpha-amylase.