Mechanism of curcumin-induced trypsin inhibition: Computational and experimental studies

In the present study, the experimental and theoretical methods were used to analyze the binding interaction of food dye , curcumin with trypsin. The results of fluorescence spectroscopic measurements indicated that curcumin binding resulted in the obviously intrinsic fluorescence quenching with the increase concentration of curcumin. This binding interaction is a spontaneous process with the estimated enthalpy and entropy changes being −15.70 kJ mol −1 and 40.25 J mol −1  K −1 , respectively. Hydrogen bonds and hydrophobic forces played an important role in the complex formation between curcumin and trypsin. Moreover, curcumin could enter into the primary substrate-binding pocket and makes the activity of trypsin decrease remarkably with the increasing concentration of curcumin.