Myricetin inhibits the generation of superoxide anion by reduced form of xanthine oxidase

Zhang, Cen; Zhang, Guowen; Liao, Yijing; Gong, Deming

doi:10.1016/j.foodchem.2016.10.136

Cited by 88 publications

(44 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Total docking was 100 times and the minimum energy was selected to find the best binding conformation of 5‐HMF–ctDNA complex. The cluster result analysis of docking was performed using a root mean square deviation tolerance of 2.0 Å …”

Section: Methodsmentioning

confidence: 69%

See 1 more Smart Citation

Exploring the binding interaction of Maillard reaction by‐product 5‐hydroxymethyl‐2‐furaldehyde with calf thymus DNA

Zhou

Zhang

et al. 2019

J Sci Food Agric

Self Cite

View full text Add to dashboard Cite

BACKGROUND 5‐Hydroxymethyl‐2‐furaldehyde (5‐HMF), a by‐product of the Maillard reaction, usually present in fried and baked food, may cause potential harm to the human body. Here, the interaction between 5‐HMF and calf thymus DNA (ctDNA) under physiological buffer (pH 7.4) was studied using multi‐spectroscopic methods combined with multivariate curve resolution–alternating least squares (MCR‐ALS) chemometrics and molecular simulation techniques. RESULTS The concentration profiles and pure spectra of the three components (5‐HMF, ctDNA and 5‐HMF–ctDNA complex) were extracted from highly overlapping spectra using MCR‐ALS analysis, which verified the formation of 5‐HMF–ctDNA complex. The binding constant being of the order of 103 L mol−1 at four temperatures (292, 298, 304 and 310 K) indicated a weak affinity in the binding of 5‐HMF to ctDNA. The binding interaction was mainly driven by hydrogen bonds and van der Waals forces. Viscosity analysis, melting assay, ionic strength effect and competitive fluorescence studies ascertained that 5‐HMF bound to ctDNA through groove binding, and it tended to bind to guanine–cytosine rich region of ctDNA which was characterized using Fourier transform infrared spectra and molecular docking. Circular dichroism spectral analysis and DNA cleavage assays indicated that the ctDNA conformation was altered from B to A form and 5‐HMF caused DNA damage at higher concentration. CONCLUSIONS The results suggested that 5‐HMF bound to ctDNA through groove binding and caused DNA damage. This research may contribute to understand the binding mechanism of 5‐HMF to ctDNA and to the assessment of the toxicological effect of 5‐HMF in biological processes. © 2018 Society of Chemical Industry

show abstract

Section: Methodsmentioning

confidence: 69%

“…To characterize the binding mode between 5‐HMF and ctDNA, computer‐aided molecular docking was used to show intuitively experimental results. According to the principle of combined energy, 100 docking run experiments were conducted . As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Exploring the binding interaction of Maillard reaction by‐product 5‐hydroxymethyl‐2‐furaldehyde with calf thymus DNA

Zhou

Zhang

et al. 2019

J Sci Food Agric

Self Cite

View full text Add to dashboard Cite

show abstract

“…The hydroxyl group at position C-5 and C-7 showed a positive contribution as the enzyme xanthine oxidase inhibitor, while the C-2' position, C-8, and C-3 will negatively contribute to the inhibition of xanthine oxidase. 18,14 Lineweaver-Burk plot and isolate obtained Michaelis-Menten constant constants (Km) of isolated compound was 9.17. These results indicated the existence of a competitive inhibition type inhibitor.…”

Section: Structure Of Isolated Compoundmentioning

confidence: 93%

Antioxidant Activity and Isolation of Xanthine Oxidase Inhibitor from Ruellia tuberosa L. Leaves

Ahmad

Elya²,

Mun’im³

2017

View full text Add to dashboard Cite

Introduction:The leaves of Ruellia tuberosa L. have been known to demonstrate strong antioxidant and xanthine oxidase (XOD) inhibitory activities. The aim of this study was to isolate antioxidant and XOD inhibitor from the leaves of the plants. Methods: Isolation of antioxidant and XOD inhibitor were conducted using chromatography techniques. The structure of the isolated compound was elucidated by spectroscopic methods. Results: In this study, a flavonoid was isolated and characterized as methoxylated flavonoid based on the spectral data including UV, IR, GC-MS, and NMR. The compound demonstrated DPPH free radical scavenging activity with IC 50 of 28.79 µg/ml, and XOD inhibitory with IC 50 of 0.67 µg/mL. Conclusion: The isolated compound was determined as 5-hydroxy-3,7-dimethoxy-2-(4-((3S,4S,5S,6R)-4,5, 6-trihydroxy-2(hydroxymethoxy)-tetrahydro-2H-pyrane-3-iloxy) phenyl)-4H-chromen-4-on or camarosids. The isolated compound demonstrated strong DPPH free radical scavenging and XOD inhibitory activity.

show abstract

“…reported myricetin ( 123 ) (IC 50 = 4.55 × 10 −6 mol L −1 ) as a mixed‐type inhibitor of XO. Molecular docking showed that it blocks the transmission of O 2 − by attaching near the binding site of isoalloxazine ring in FAD domain; hydrogen peroxide thus formed by the transfer of electron from FADH 2 to O 2 − . Gawlik‐Dziki and colleagues studied the phenolic contents and in vitro XO inhibitory activity of wholemeal wheat flour and green coffee beans.…”

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

View full text Add to dashboard Cite

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.

show abstract

Myricetin inhibits the generation of superoxide anion by reduced form of xanthine oxidase

Cited by 88 publications

References 39 publications

Exploring the binding interaction of Maillard reaction by‐product 5‐hydroxymethyl‐2‐furaldehyde with calf thymus DNA

Exploring the binding interaction of Maillard reaction by‐product 5‐hydroxymethyl‐2‐furaldehyde with calf thymus DNA

Antioxidant Activity and Isolation of Xanthine Oxidase Inhibitor from Ruellia tuberosa L. Leaves

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

Contact Info

Product

Resources

About