文章基本信息

标题：In vitro Inhibition of Pancreatic Lipase by Polyphenols: A Kinetic, Fluorescence Spectroscopy and Molecular Docking Study
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作者：Martinez-Gonzalez, Alejandra I. ; Alvarez-Parrilla, Emilio ; Díaz-Sánchez, Ángel G. 等
期刊名称：Food Technology and Biotechnology
印刷版ISSN：1330-9862
电子版ISSN：1334-2606
出版年度：2017
卷号：55
期号：4
页码：519-530
DOI：10.17113/ftb.55.04.17.5138
语种：English
出版社：Sveuciliste u Zagrebu - Faculty of Food
摘要：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.
关键词：polyphenolic compounds; pancreatic lipase; enzymatic inhibition; molecular docking; anti-obesity effect