Flavonoid binding to human serum albumin

作者：Bolli Alessandro; Marino Maria; Rimbach Gerald; F****i Gabriella; Fasano Mauro; Ascenzi Paolo^*

来源：Biochemical and Biophysical Research Communications, 2010, 398(3): 444-449.

DOI：10.1016/j.bbrc.2010.06.096

• Human serum albumin
• Flavonoid binding
• Daidzein
• Daidzein metabolites
• Genistein
• Naringenin
• Quercetin
• Oleate
• Thermodynamics
• Allostery

Dietary flavonoid may have beneficial effects in the prevention of chronic diseases. However, flavonoid bioavailability is often poor probably due to their interaction with plasma proteins. Here, the affinity of daidzein and daidzein metabolites as well as of genistein, naringenin, and quercetin for human serum albumin (HSA) has been assessed in the absence and presence of oleate. Values of the dissociation equilibrium constant (K) for binding of flavonoids and related metabolites to Sudlow's site I range between 3.3 x 10(-6) and 3.9 x 10(-5) M, at pH 7.0 and 20.0 degrees C, indicating that these flavonoids are mainly bound to HSA in vivo. Values of K increase (i.e., the flavonoid affinity decreases) in the presence of saturating amounts of oleate by about two folds. Present data indicate a novel role of fatty acids as allosteric inhibitors of flavonoid bioavailability, and appear to be relevant in rationalizing the interference between dietary compounds, food supplements, and drugs.

• 出版日期2010-7-30