Study of the binding mechanism between hydroxytyrosol and bovine serum albumin using multispectral and molecular docking

Abstract Hydroxytyrosol (HT) is a naturally occurring amphiphilic plant polyphenol with tremendous potential as an antioxidant, antibacterial, anti-cancer, cardiovascular disease treatment, etc. However, the mechanisms of its interactions with proteins remain unclear. The interaction between HT and bovine serum albumin (BSA) in vitro was investigated through multispectral spectroscopy, molecular docking, particle size studies, and atomic force microscopy (AFM). Fluorescence spectra and molecular docking results indicated that HT was bound to the active site of BSA via hydrophobic forces through a spontaneous binding process (ΔG