Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 57, Issue 15, Pages 6642-6648Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf901456u
Keywords
Affinity; flavonoid glycosides; glycosylation; plasma protein
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The interaction between flavonoids and proteins has attracted great interest among researchers, However, few reports have focused on the structure-affinity relationship of flavonoids binding to proteins. This work mainly concerns the effect of glycosylation of flavonoids on the affinities for BSA. Four flavonoid aglycones (baicalein, quercetin, daidzein, and genistein) and their monoglycosides (baicalin, quercitrin, daidzin, and puerarin, genistin) and another poly glycoside (rutin) are studied for their affinities for BSA. The glycosylation of flavonoids significantly affects the quenching/binding process. In general, the glycosylation of flavonoids lowers the affinity for BSA by 1 to 3 orders of magnitude depending on the conjugation site and the class of sugar moiety. The glucopyranosylation (daidzin and genistin) of flavonoids lowered the affinity for BSA by 5-10 times. Rhamnosylation (quercitrin) of flavonoids, however, lowered the affinity for BSA by 5600 times. This result partly supports that flavonoid aglycones are more easily absorbed than flavonoid glycosides. Higher binding affinities for BSA are associated with higher antioxidant activities for flavonoids. Glycosylation also decreases the hydrophobicity of flavonoids, and hydrophobic interaction may play an important role in binding flavonoids to proteins.
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