In vitro Inhibition of Pancreatic Lipase by Polyphenols: A Kinetic, Fluorescence Spectroscopy and Molecular Docking Study

Alejandra I. Martinez-Gonzalez1orcid tiny, Emilio Alvarez-Parrilla1*orcid tiny, Ángel G. Díaz-Sánchez1orcid tiny,
Laura A. de la Rosa1orcid tiny, José A. Núñez-Gastélum1orcid tiny, Alma A. Vazquez-Flores1orcid tiny and Gustavo A. Gonzalez-Aguilar2orcid tiny

1Department of Chemical Biological Sciences, Institute for Biomedical Sciences, Autonomous University of
Juarez City, 1210 Plutarco Elias Calles Ave., MX-32310 Juarez, Chihuahua, Mexico
2Research Center for Food and Development, A.C. (CIAD), Carretera a Ejido La Victoria, Km. 0.6,
MX-83304 Hermosillo, Sonora, Mexico

Article history:
Received: January 1, 2017
Accepted: September 7, 2017

Key words:
polyphenolic compounds, pancreatic lipase, enzymatic inhibition, molecular docking, anti-obesity effect


The inhibitory activity and binding characteristics of caffeic acid, p-coumaric acid, quercetin and capsaicin, four phenolic compounds found in hot pepper, against porcine pancreatic lipase activity were studied and compared to hot pepper extract. Quercetin was the strongest inhibitor (IC50=(6.1±2.4) μM), followed by p-coumaric acid ((170.2±20.6) μM) and caffeic acid ((401.5±32.1) μM), while capsaicin and a hot pepper extract had very low inhibitory activity. All polyphenolic compounds showed a mixed-type inhibition. Fluorescence spectroscopy studies showed that polyphenolic compounds had the ability to quench the intrinsic fluorescence of pancreatic lipase by a static mechanism. The sequence of Stern-Volmer constant was quercetin, followed by caffeic and p-coumaric acids. Molecular docking studies showed that caffeic acid, quercetin and p-coumaric acid bound near the active site, while capsaicin bound far away from the active site. Hydrogen bonds and π-stacking hydrophobic interactions are the main pancreatic lipase-polyphenolic compound interactions observed. 

*Corresponding author:  tel3/fax2  +52 656 6881 894 ext. 1562