Influence of Polyphenol-plasma Protein Interaction on the Antioxidant Properties of Polyphenols

Zou, Dengfeng; Xie, Aize

doi:10.2174/1389200211314040008

Cited by 14 publications

(7 citation statements)

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“…Previous investigations have indicated that the patterns of the hydroxyl and methoxyl groups on the rings of flavonoids are involved in the bioactivities and binding affinities for proteins. − The effects of hydroxylation of flavonoids on their affinities for XO and XO inhibition are shown in Table . Baicalein with an extra C6–OH exhibited 9.84 times lower XO inhibition than chrysin, but their affinities did not change too much, indicating that the hydroxylation on the C6 (ring A) of flavones weakened the inhibitory activity obviously and the binding affinities slightly.…”

Section: Results and Discussionmentioning

confidence: 99%

Dietary Flavonoids as Xanthine Oxidase Inhibitors: Structure–Affinity and Structure–Activity Relationships

Lin

Zhang

Liao

et al. 2015

J. Agric. Food Chem.

183

120

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The flavonoid family has been reported to possess a high potential for inhibition of xanthine oxidase (XO). This study concerned the structural aspects of inhibitory activities and binding affinities of flavonoids as XO inhibitors. The result indicated that the hydrophobic interaction was important in the binding of flavonoids to XO, and the XO inhibitory ability increased generally with increasing affinities within the class of flavones and flavonols. The planar structure and the C2═C3 double bonds of flavonoids were advantageous for binding to XO and for XO inhibition. Both the hydroxylation on ring B and the substitution at C3 were unfavorable for XO inhibition more profoundly than their XO affinity. The methylation greatly reduced the inhibition (0.75-3.07 times) but hardly affected the affinity. The bulky sugar substitutions of flavonoids decreased the inhibition (1.69-1.99 times) and lowered the affinities (4.20-9.22 times) to different degrees depending on the conjunction site.

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Section: Results and Discussionmentioning

confidence: 99%

Dietary Flavonoids as Xanthine Oxidase Inhibitors: Structure–Affinity and Structure–Activity Relationships

Lin

Zhang

Liao

et al. 2015

J. Agric. Food Chem.

183

120

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“…Previous studies have proven that the patterns of the hydroxyl and methoxyl groups on both of the A and B rings of avonoids are closely related to the bioactivities and binding affinities for proteins. [32][33][34][35] The effects of hydroxylation and methoxylation of avonoids on the affinities and AChE inhibitory activities are shown in Table 2. It is noted that the hydroxylation on both ring A and ring B increased the inhibitory activities of avonoids against AChE, while methoxylation may decrease or increase the activities depending on classes of avonoids.…”

Section: Quenching Effect Of Avonoids On Ache Uorescencementioning

confidence: 99%

Inhibition of flavonoids on acetylcholine esterase: binding and structure–activity relationship

et al. 2014

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The inhibitory effects of flavonoids on acetylcholinesterase (AChE) have attracted great interest among researchers. However, few reports have focused on the structure-activity relationship for AChE inhibition of flavonoids. This work mainly concerns the structural aspects of inhibitory activities and binding affinities of flavonoids as AChE inhibitors. The results show that hydroxyl groups in the A ring of flavonoids are favorable for inhibiting AChE, and the hydroxylation increases the affinities for AChE. However, methoxylation may decrease or increase the activities depending on the class of flavonoids. The glycosylation decreases the AChE inhibitory activities of flavonoids and lowers the affinities for AChE by 1 to 5 times depending on the conjunction site and the type of sugar moiety. The hydrogenation of the C2-C3 double bond of apigenin decreases both the affinity for AChE and AChE inhibition. The molecular property-affinity relationship reveals that the hydrogen bond force plays an important role in binding flavonoids to AChE. The AChE inhibitions generally increase with the increasing affinities of flavonoids within the class, especially for flavones and flavonols.

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“…Another study by Cao et al illustrated that plasma proteins masked most of the investigated dietary polyphenols, thus reducing their radical scavenging potential; however, the results among the four employed antioxidant assays were quite different [12]. Zou reviewed the influence of polyphenol-plasma protein interaction (PpPI) on the antioxidant activity of polyphenols, and pointed out that the influence of PpPI on the antioxidant activity of polyphenols showed different trends which were decided by both the kinds of antioxidant assay and polyphenols [13]. In fact, the results obtained from different antioxidant assays were hardly comparable because of the different mechanisms, pH and solvent [14].…”

Section: Introductionmentioning

confidence: 99%

Influence of Bovine Serum Albumin-Flavonoid Interaction on the Antioxidant Activity of Dietary Flavonoids: New Evidence from Electrochemical Quantification

Geng

Liu

et al. 2018

Molecules

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Interaction between dietary flavonoids and albumins plays an important role in the bioavailability and bioactivity of flavonoids. Therefore, the influence of this interaction on the antioxidant activity of flavonoid has attracted much interest. In this study, a ceric reducing/antioxidant capacity assay (CRAC) was employed to investigate the effects of albumin-flavonoid interaction on the antioxidant activity of seven common flavonoids. The results obtained from the CRAC assay were also compared separately with the results from the spectrophotometric methods including 2,2-diphenyl-1-picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) assays. All the flavonoids show a decreasing in the antioxidant activity detected by CRAC assay, indicting a “masking effect” of bovine serum albumin (BSA)-flavonoid interaction. However, the results from DPPH and FRAP assays were conflicting, which may be attributed to the influence of solvent systems.

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Influence of Polyphenol-plasma Protein Interaction on the Antioxidant Properties of Polyphenols

Cited by 14 publications

References 0 publications

Dietary Flavonoids as Xanthine Oxidase Inhibitors: Structure–Affinity and Structure–Activity Relationships

Dietary Flavonoids as Xanthine Oxidase Inhibitors: Structure–Affinity and Structure–Activity Relationships

Inhibition of flavonoids on acetylcholine esterase: binding and structure–activity relationship

Influence of Bovine Serum Albumin-Flavonoid Interaction on the Antioxidant Activity of Dietary Flavonoids: New Evidence from Electrochemical Quantification

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