Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 51, Issue 12, Pages 3555-3561Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jm800115x
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In this study we investigated the structural requirements for inhibition of human salivary alpha-amylase by flavonoids. Four flavonols and three flavones, out of the 19 flavonoids tested, exhibited IC50 values less than 100 mu M against human salivary alpha-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 pi-system that stabilizes the interaction with the active site. Our findings show that certain naturally occurring flavonoids act as inhibitors of human a.-amylase, which makes them promising candidates for controlling the digestion of starch and postprandial glycemia.
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