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

ABSTRACT: 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 dockin

SUBMITTER: Martinez-Gonzalez AI 

PROVIDER: S-EPMC5848196 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature