Hui Wang

Government of the People's Republic of China, Peping, Beijing, China

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Publications (3)10.54 Total impact

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    ABSTRACT: The influence of glucose on the interaction between flavonoids and plasma proteins from healthy human (HPP) was investigated. Glucose affected the flavonoid-protein interaction depending on their structures. Glucose significantly reduced the affinities of HPP for 6-hydroxyflavone by 10.72 times, slightly weakened the affinities of HPP for quercetin, 7-hydroxyflavone, and kaempferol, and hardly affected the affinities of HPP for myricetin, chrysin and 3,7-dihydroxyflavone on the first day. However, glucose obviously enhanced the affinities of HPP for 3-hydroxyflavone, luteolin and apigenin. Glucose significantly weakened the binding affinities of HPP for chrysin, kaempferol, quercetin, and myricetin by 6.17, 7.94, 14.12, and 112.2 times, when kept at 37 °C under air condition for 14 days and the binding affinities of HPP for 7-hydroxyflavone, luteolin, 3,7-dihydroxyflavone, 3-hydroxyflavone, and 6-hydroxyflavone were slightly decreased by 1.35, 1.58, 1.58, 1.9, and 2.4-fold, and the binding affinity between apigenin and HPP was hardly influenced. Glucose weakened the binding affinities of HPP for hydroxyflavonoids and the differences between lgKa(absence) and lgKa(presence) were bigger for the more lipophilic hydroxyflavonoids and more lipophilic hydroxyflavonoids are easily affected by glucose, when kept at 37 °C under air condition for 14 days. These flavonoids with lower hydrogen donor/acceptor numbers prefer to stable interact with HPP in the presence of glucose. However, other flavonoids with high hydrogen donor/acceptor numbers (multi-hydroxyl flavonoids) were apt to reduce their affinities with HPP in the presence of glucose.
    Journal of Agricultural and Food Chemistry 11/2012; · 3.11 Impact Factor
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    ABSTRACT: The molecular structure/property-affinity relationships of dietary polyphenols non-covalently binding to total plasma proteins of type II diabetes (IIDTPP) were investigated by comparing the binding constants obtained from the fluorescence titration method. An additional methoxy group in flavonoids increased their binding affinities for IIDTPP by 1.38 to 15.85 times. The hydroxylation at the 4' position (Ring B) of flavonols and the 5 position (Ring A) of isoflavones weakened the binding affinities; however, hydroxylation at other positions on flavonoids slightly enhanced or little affected the binding affinities for IIDTPP. The glycosylation of flavonoids slightly decreased or little affected the affinities for IIDTPP by less than 1 order of magnitude. The hydrogenation of the C2[double bond, length as m-dash]C3 double bond of flavone, 6-hydroxyflavone, 6-methoxyflavone and myricetin decreased the binding affinities. The galloylation of catechins significantly improved the binding affinities with IIDTPP approximately 10 to 1000 times. The esterification of gallic acid increased its binding affinity. The hydrophobic force played an important role in the binding interaction between polyphenols and IIDTPP.
    Integrative Biology 09/2011; 3(11):1087-94. · 4.32 Impact Factor
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    ABSTRACT: Common human plasma proteins (CHPP), also called blood proteins, are proteins found in blood plasma. The molecular structure/property-affinity relationships of dietary polyphenols noncovalently binding to CHPP were investigated by comparing the binding constants obtained from the fluorescence titration method. An additional methoxy group in flavonoids increased their binding affinities for CHPP by 1.05 to 72.27 times. The hydroxylation on the 4' position (ring B) of flavones and flavonols and the 5 position (ring A) of isoflavones weakened the binding affinities; however, the hydroxylation on other positions of flavonoids slightly enhanced or little affected the binding affinities for CHPP. The glycosylation of flavonoids weakened or slightly affected the affinities for CHPP by 1 order of magnitude. The hydrogenation of the C2═C3 double bond of flavone, 6-hydroxyflavone, 6-methoxyflavone and myricetin decreased the binding affinities about 10.02 to 17.82 times. The galloylation of catechins significantly improved the binding affinities with CHPP about 10 to 1000 times. The esterification of gallic acid increased its binding affinity. The binding affinities with CHPP were strongly influenced by the structural differences of dietary polyphenols. Polyphenols with higher affinities for purified HSA also showed stronger affinities with CHPP. The hydrophobic force played an important role in binding interaction between polyphenols and CHPP.
    Journal of Agricultural and Food Chemistry 08/2011; 59(19):10747-54. · 3.11 Impact Factor