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BIOANALYTICAL

Comparing the Affinities of Flavonoid Isomers with Protein by Fluorescence Spectroscopy

, , , &
Pages 521-532 | Received 10 Nov 2007, Accepted 01 Dec 2007, Published online: 31 Mar 2008
 

Abstract

Dietary flavonoids can be detected in plasma as protein‐bound conjugates. Flavonoids–protein interaction is expected to modulate the bioavailability of flavonoids. In this work, the binding flavonoid isomers (galangin, baicalein, apigenin, and genistein; MW=270.25) and B‐ring hydroxylation flavonols (galangin, kaempferol, quercetin, and myricetin, which share the same structure on the A and C rings but have 0, 1, 2, and 3 moieties of ‐OH on the B‐ring, respectively) to protein were investigated by fluorescence quenching method. The apparent binding constants (K a ) of were flavonoid isomers determined as: flavones (106–107 L mol−1)>isoflavone≈flavonol (105 L mol−1). For B‐ring hydroxylation flavonols, the binding affinity increased with increasing number of hydroxyl groups on the B‐ring. The binding constants (K a ) were determined as follows: myricetin>quercetin>kaempferol>galangin.

The authors are grateful for financial support from the Natural Science Research Project of Nantong University (grant No. 06Z021) and Natural Science Basic Research Project of Jiangsu Province University (grant No. 05KJD430163 and BK2006545).

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