Comparative study of the binding between chlorogenic acid and four proteins by isothermal titration calorimetry, spectroscopy and docking methods

Abstract As a polyphenolic compound, chlorogenic acid has antioxidant, anti-inflammatory, antiviral, anti-obesity and other effects. Based on the interactions between chlorogenic acid and the proteins (human serum albumin (HSA), pepsin (Pep), trypsin (Try), fat mass and obesity-associated protein (FTO)), results will provide clues for screening effective inhibitors. The interaction between chlorogenic acid and the four proteins (HSA, Pep, Try, FTO) was analyzed by the aid of fluorescence quenching, synchronous fluorescence, three-dimensional fluorescence, isothermal titration calorimetry, and molecular docking. It can be concluded that there is no obvious interaction between chlorogenic acid and FTO. The binding affinity between chlorogenic acid and three proteins is HSA > Try > Pep. The binding process is spontaneous, and the quenching type is static quenching. Hydrophobic interaction and hydrogen bonding is observed in the binding process. This study provides valuable information for understanding the interaction mechanism between chlorogenic acid and proteins, and provides clues for screening inhibitors. Graphical abstract