Mechanism of action and interactions between xanthine oxidase inhibitors derived from natural sources of chlorogenic and ferulic acids

Gawlik‐Dziki, Urszula; Dziki, Dariusz; Świeca, Michał; Nowak, Renata

doi:10.1016/j.foodchem.2017.01.016

Cited by 57 publications

(32 citation statements)

References 32 publications

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“…SA enters the active site of XOD enzyme and forms a hydrogen bond with the surrounding amino acids, altering the XOD structure and further thwarting the entrance of the substrate (hypoxanthine/xanthine) to XOD, thus inhibiting uric acid synthesis A similar inhibitory mode has been observed in various bioactive compounds Gawlik-Dziki et al, 2017;Lin et al, 2015;Pathak et al, 2018;Zhang et al, 2016 Herein, SA downregulated SUA and increased UUA levels. *p < .05, **p < .01, ***p < .001 compared with normal control and # p < .05, ## p < .01, ### p < .001 compared with PC F I G U R E 1 2 Proposed xanthine oxidase (XOD) inhibitory mechanism of sinapic acid (SA).…”

Section: F I G U R E 11mentioning

confidence: 63%

Antihyperuricemic effect of dietary polyphenol sinapic acid commonly present in various edible food plants

et al. 2019

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The present study was conducted to evaluate the antihyperuricemic effect of sinapic acid (SA). The results showed that SA potently inhibited xanthine oxidase (XOD) in a dose-dependent manner by entering the enzyme active site and thwarting the entrance of the substrate. These results were further confirmed by the quantum chemical descriptors analysis and 1 H NMR titration analysis. The in vivo results indicated that SA not only has the potential to inhibit serum and hepatic XOD (p < .05), but also remarkably lowered serum and urine uric acid levels at 50 and 100 mg/kg bw.Furthermore, SA regulated serum creatinine and blood urea nitrogen levels to normal and lowered inflammation in the renal tubules. Thus, the utilization of SA as an antihyperuricemic agent may have considerable potential for the development of functional foods for the possible treatment of hyperuricemia.

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Section: F I G U R E 11mentioning

confidence: 63%

Antihyperuricemic effect of dietary polyphenol sinapic acid commonly present in various edible food plants

et al. 2019

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“…Both CRA and myricetin individually could inhibit α ‐glucosidase. To determine their combined inhibition, a dose‐normalized isobologram was employed following Gawlik–Dziki's method . The activity of α ‐glucosidase was evaluated in the same way as in α‐Glucosidase activity assay.…”

Section: Methodsmentioning

confidence: 99%

“…To determine their combined inhibition, a dose-normalized isobologram was employed following Gawlik-Dziki's method. 29 The activity of -glucosidase was evaluated in the same way as in -Glucosidase activity assay. The doses of myricetin were kept constant (0.2, 0.6 and 0.8 × 10 −6 mol L −1 ), and various amounts of CRA were subsequently added to attain 30%, 50%, and 70% inhibition in the combination of two agents.…”

Section: Isobolographic Analysismentioning

confidence: 99%

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Pan

et al. 2019

J Sci Food Agric

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BACKGROUND The suppression of α‐glucosidase activity to retard glucose absorption is an important therapy for type‐2 diabetes. Corosolic acid (CRA) is a potential antidiabetic component in many plant‐based foods and herbs. In this study, the interplay mechanism between α‐glucosidase and corosolic acid was investigated by several methods, including three‐dimensional fluorescence spectra, circular dichroism spectra, and molecular simulation. RESULTS Corosolic acid significantly inhibited α‐glucosidase reversibly in an uncompetitive manner and its IC50 value was 1.35 × 10−5 mol L−1. A combination of CRA with myricetin exerted a weak synergy against α‐glucosidase. The intrinsic fluorescence of α‐glucosidase was quenched via a static quenching course and the binding constant was 3.47 × 103 L mol−1 at 298 K. The binding of CRA to α‐glucosidase was mainly driven by hydrophobic forces and resulted in a partial extension of the protein polypeptide chain with a loss of α‐helix content. The molecular simulation illustrated that CRA bound to the entrance part of the active center of α‐glucosidase and interacted with the amino acid residues Ser157, Arg442, Phe303, Arg315, Tyr158, and Gln353, which could hinder the release of substrate and catalytic reaction product, eventually suppressing the catalytic activity of α‐glucosidase. CONCLUSIONS These results may suggest new insights into corosolic acid from food sources as a potential α‐glucosidase inhibitor that could better control diabetes. © 2019 Society of Chemical Industry

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“…Gawlik‐Dziki and colleagues studied the phenolic contents and in vitro XO inhibitory activity of wholemeal wheat flour and green coffee beans. It was found that presence of trans ‐ and cis ‐ferulic acids in wheat flour and 5‐caffeoylquinic acid in green coffee beans showed good inhibition of XO . Wang and his co‐workers identified 11 compounds from Perilla frutescens as XO inhibitors.…”

Section: Xanthine Oxidasementioning

confidence: 99%

Toward an Understanding of Structural Insights of Xanthine and Aldehyde Oxidases: An Overview of their Inhibitors and Role in Various Diseases

Kumar

Joshi

Kler

et al. 2017

Medicinal Research Reviews

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Almost all drug molecules become the substrates for oxidoreductase enzymes, get metabolized into more hydrophilic products and eliminated from the body. These metabolites sometime may be more potent, active, inactive, or toxic in nature compared to parent molecule. Xanthine oxidoreductase and aldehyde oxidase belong to molybdenum containing family and are well characterized for their structures and functions, in particular to their ability to oxidize/hydroxylate the xenobiotics. Their upregulated clinical levels causing oxidative stress are associated with pathways either directly involved in the progression of diseases, gout, or indirectly with the succession of other diseases such as diabetes, cancer, etc. Herein, we have put forth a comprehensive review on the xanthine and aldehyde oxidases pertaining to their structures, functions, pathophysiological role, and a comparative analysis of structural insights of xanthine and aldehyde oxidases' binding domains with endogenous ligands or inhibitors. Though both the enzymes are molybdenum containing and are likely to share some common pathways and interact with inhibitors in a similar manner but we have focused on structural prerequisites for inhibitor specificity to both the enzymes keeping in view of the existing X-ray structures. This review also provides futuristic implications in the design of inhibitors derived from inorganic complexes or small organic molecules considering the spatial features and structural insights of both the enzymes.

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Mechanism of action and interactions between xanthine oxidase inhibitors derived from natural sources of chlorogenic and ferulic acids

Cited by 57 publications

References 32 publications

Antihyperuricemic effect of dietary polyphenol sinapic acid commonly present in various edible food plants

Antihyperuricemic effect of dietary polyphenol sinapic acid commonly present in various edible food plants

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Toward an Understanding of Structural Insights of Xanthine and Aldehyde Oxidases: An Overview of their Inhibitors and Role in Various Diseases

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