A novel approach to trypsin inhibition by flavonoids

Trypsin is a key protease related to digestion and absorption of proteins, which its inhibition must be studied when natural compounds, such as flavonoids, are used part alternative treatments for obesity diabetes mellitus type 2, since trypsin together with other pancreatic enzymes worked at small intestine. Considering that flavonoids good lipase amylase inhibitors, trypsin-flavonoids interactions were analyzed through UV-Vis, intrinsic extrinsic fluorescence spectroscopies, circular dichroism, molecular docking. The interaction between porcine pancreas five flavonoids: hesperetin (HES), luteolin (LUT), quercetin (QUE), catechin (CAT), rutin (RUT) was evaluated. Most them exhibited mixed-type mode. LUT the best inhibitor (e.g., lower IC50, 45.20±1.00 µM). All flavonoids-trypsin complexes showed static quenching, QUE higher affinity (higher Ka values, 0.90±0.10 1.60±0.20·10-1 mM-1, respectively). Hydrophobic predominant.