Comparing the affinities of flavonoid isomers with protein by fluorescence spectroscopy Journal Article


Authors: Cao, H.; Liu, Q.; Shi, J.; Xiao, J.; Xu, M.
Article Title: Comparing the affinities of flavonoid isomers with protein by fluorescence spectroscopy
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 (Ka) 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 (Ka) were determined as follows: myricetin > quercetin > kaempferol > galangin. Copyright © Taylor & Francis Group, LLC.
Keywords: fluorescence quenching; bovine serum albumin; bovinae; flavonoid isomer; flavonol
Journal Title: Analytical Letters
Volume: 41
Issue: 4
ISSN: 0003-2719
Publisher: Taylor & Francis Group  
Date Published: 2008-01-01
Start Page: 521
End Page: 532
Language: English
DOI: 10.1080/00032710801910486
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 13" - "Export Date: 17 November 2011" - "CODEN: ANALB" - "Source: Scopus"
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  1. Ming Xu
    16 Xu