In vitro and in silico studies to explore structural features of flavonoids for aldehyde oxidase inhibition.
Maryam Hamzeh-Mivehroud, Seifullah Rahmani, Mohammad-Ali Hosseinpour Feizi, Siavoush Dastmalchi, Mohammad-Reza Rashidi
Index: Arch. Pharm. (Weinheim) 347(10) , 738-47, (2014)
Full Text: HTML
Abstract
Aldehyde oxidase (AO), an important enzyme in the biotransformation of drugs and xenobiotics, is inhibited by flavonoids. This enzyme can metabolize both aldehydes and N-heterocycles. In this work, a set of 15 flavonoids was assessed for inhibitory activity on the AO oxidation of vanillin as an aldehyde substrate. Spectrophotometrically determined IC50 values showed that myricetin, quercetin, and epicatechin were the most potent inhibitors. The results also revealed that the inhibition of vanillin oxidation by flavonoids was stronger than that of phenanthridine oxidation (an N-heterocyclic substrate) as reported previously. In order to investigate the important structural features responsible for the inhibitory effects of the studied flavonoids, a quantitative structure-activity relationship (QSAR) analysis was performed. This study showed that the size of the flavonoids was the most important factor inversely affecting their potencies. The QSAR model can be used more broadly to predict the AO inhibitory activity of flavonoid-like structures for application in food-drug and drug-drug interaction studies. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Related Compounds
Related Articles:
2015-01-01
[PLoS ONE 10 , e0132429, (2015)]
2015-01-01
[PLoS ONE 10 , e0132791, (2015)]
The antioxidant and antigenotoxic properties of citrus phenolics limonene and naringin.
2015-07-01
[Food Chem. Toxicol. 81 , 160-70, (2015)]
Polyphenolic Profile of Pear Leaves with Different Resistance to Pear Psylla (Cacopsylla pyri).
2015-09-02
[J. Agric. Food Chem. 63 , 7476-86, (2015)]
2014-08-27
[J. Agric. Food Chem. 62(34) , 8764-71, (2014)]