Flavonoid binding to human serum albumin

被引:118
作者
Bolli, Alessandro [1 ]
Marino, Maria [1 ]
Rimbach, Gerald [2 ]
Fanali, Gabriella [3 ,4 ]
Fasano, Mauro [3 ,4 ]
Ascenzi, Paolo [1 ,5 ]
机构
[1] Univ Roma Tre, Dept Biol, I-00146 Rome, Italy
[2] Univ Kiel, Inst Human Nutr & Food Sci, D-24098 Kiel, Germany
[3] Univ Insubria, Dept Struct & Funct Biol, I-21052 Busto Arsizio, VA, Italy
[4] Univ Insubria, Ctr Neurosci, I-21052 Busto Arsizio, VA, Italy
[5] Univ Roma Tre, Interdept Lab Electron Microscopy, I-00146 Rome, Italy
关键词
Human serum albumin; Flavonoid binding; Daidzein; Daidzein metabolites; Genistein; Naringenin; Quercetin; Oleate; Thermodynamics; Allostery; DRUG-BINDING; CRYSTAL-STRUCTURE; CRYSTALLOGRAPHIC ANALYSIS; ALLOSTERIC MODULATION; AUTOMATED DOCKING; LIGAND-BINDING; FATTY-ACIDS; ANTIOXIDANT; WARFARIN; COMPETITION;
D O I
10.1016/j.bbrc.2010.06.096
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2010 Elsevier Inc. All rights reserved.
引用
收藏
页码:444 / 449
页数:6
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