Flavonoids for Controlling Starch Digestion: Structural Requirements for Inhibiting Human α-Amylase

Elena Lo Piparo*‡, Holger Scheib‡, Nathalie Frei, Gary Williamson, Martin Grigorov and Chieh Jason Chou
Nestl Research Center, Vers-chez-les-Blanc, P.O. Box 44, CH-1000 Lausanne 26, Switzerland
J. Med. Chem., 2008, 51 (12), pp 3555–3561
DOI: 10.1021/jm800115x
Publication Date (Web): May 29, 2008
Copyright © 2008 American Chemical Society
* To whom correspondence should be addressed. Telephone: +41-(0)21-785-9530 . Fax: +41-(0)21-785-9486. E-mail: elena.lopiparo@rdls.nestle.com.
,
‡

These authors contributed equally to this work.

Abstract

Abstract Image

In this study we investigated the structural requirements for inhibition of human salivary α-amylase by flavonoids. Four flavonols and three flavones, out of the 19 flavonoids tested, exhibited IC50 values less than 100 µM against human salivary α-amylase activity. Structure−activity relationships of these inhibitors by computational ligand docking showed that the inhibitory activity of flavonols and flavones depends on (i) hydrogen bonds between the hydroxyl groups of the polyphenol ligands and the catalytic residues of the binding site and (ii) formation of a conjugated π-system that stabilizes the interaction with the active site. Our findings show that certain naturally occurring flavonoids act as inhibitors of human α-amylase, which makes them promising candidates for controlling the digestion of starch and postprandial glycemia.

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History

  • Published In Issue June 26, 2008
  • Article ASAPMay 29, 2008
  • Received: February 04, 2008

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