Interaction of eugenol with xanthine oxidase: Multi spectroscopic and in silico modelling approach

Vijeesh, V; Jisha, Ninan; Vysakh, A.; Latha, M.S.

doi:10.1016/j.saa.2021.119843

Cited by 12 publications

(7 citation statements)

References 27 publications

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“…The fluorescence intensity of XO decreased due to the concentration of luteoloside increased, 34 indicating that luteoloside interacted with XO and affected the inherent structure of the enzyme protein, which quenched its inherent fluorescence 35 . Vijeesh et al found that the fluorescence intensity of XO decreased as the concentration of eugenol increased, which was similar to our results 22 …”

Section: Resultssupporting

confidence: 91%

“…35 Vijeesh et al found that the fluorescence intensity of XO decreased as the concentration of eugenol increased, which was similar to our results. 22 The type of quenching was calculated by Equation (2). 36,37…”

Section: Fluorescence Quenching Mechanismmentioning

confidence: 99%

“…19 Eugenol has anti-inflammatory and anti-cancer activities, 20,21 which can combine with XO and change the conformation of XO. 22 Therefore, the study of interaction and binding mode between flavonoids and enzyme proteins can provide valuable information for the investigation of the activity of drug molecules. 23 At present, due to the accuracy, sensitivity, and easy operation, multispectral analysis technology has become the main tool to study the interaction mode between ligand and protein.…”

Section: Introductionmentioning

confidence: 99%

“…Luteolin can effectively inhibit the activity of XO, 11 and apigenin can combine with XO to change the structure of XO, 17,18 which significantly inhibits the activity of XO 19 . Eugenol has anti‐inflammatory and anti‐cancer activities, 20,21 which can combine with XO and change the conformation of XO 22 . Therefore, the study of interaction and binding mode between flavonoids and enzyme proteins can provide valuable information for the investigation of the activity of drug molecules 23 …”

Section: Introductionmentioning

confidence: 99%

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Study on the interaction mechanism between luteoloside and xanthine oxidase by multi‐spectroscopic and molecular docking methods

Chen

Wang

Pan

et al. 2022

J of Molecular Recognition

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Gout is an inflammatory joint disease caused by urate crystal deposition, which is associated with hyperuricemia. Gout will take place when the uric acid accumulates. Xanthine oxidase (XO) is a crucial enzyme in the formation of uric acid. Inhibiting XO is one of the means to ameliorate gout. Luteoloside is a kind of natural flavonoid, which has an excellent prospect for relieving gout. But there are few reports on the interaction mechanism between luteoloside and XO currently. In this study, the interaction mechanism between luteoloside and XO was explored using spectroscopy and molecular docking. The fluorescence spectroscopy results indicated that luteoloside could make the intrinsic fluorescence of XO quenched, and the binding constant between luteoloside and XO was (1.85 ± 0.22) × 103 L mol−1 at 298 K. The synchronous fluorescence spectroscopy results showed that the absorption peaks of Tyr and Trp shifted blue, and the hydrophobicity of the microenvironment increased. Moreover, CD spectra showed that α‐helix of XO decreased, β‐sheet and β‐turn increased after adding luteoloside. The results of molecular docking analysis showed that XO could combine with luteoloside through hydrogen bonds and hydrophobic force. The results indicated that luteoloside could remarkably interact with XO. Insights into the interaction mechanism provide a necessary basis for the search for low‐toxic natural products as targets of XO. Highlights Luteoloside and xanthine oxidase was a strong binding mode and had only one binding site. Luteoloside could cause α‐helix reduced, β‐sheet and β‐turn increased, and change the secondary structure of XO. The binding between luteoloside and xanthine oxidase was a spontaneous process. The main binding force was hydrophobic force between luteoloside and xanthine oxidase.

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Section: Resultssupporting

confidence: 91%

Section: Fluorescence Quenching Mechanismmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Study on the interaction mechanism between luteoloside and xanthine oxidase by multi‐spectroscopic and molecular docking methods

Chen

Wang

Pan

et al. 2022

J of Molecular Recognition

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“…The CD spectra of XO in the presence of different molar ratios of ECG to XO were measured to analyze the secondary structure of XO. As shown in Figure 4A, an obvious negative absorption band was observed at around 216 nm for XO, which denoted the characteristic band of β-sheet structure [52]. With the increase of the molar ratio of ECG to XO, the intensity of the CD band increased, and the shape and position of the characteristic peak shifted significantly, which implied that ECG induced the conformational alterations of XO.…”

Section: Spectra Studiesmentioning

confidence: 91%

Epicatechin Gallate as Xanthine Oxidase Inhibitor: Inhibitory Kinetics, Binding Characteristics, Synergistic Inhibition, and Action Mechanism

Zhu

Pan

et al. 2021

Foods

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Epicatechin gallate (ECG) is one of the main components of catechins and has multiple bioactivities. In this work, the inhibitory ability and molecular mechanism of ECG on XO were investigated systematically. ECG was determined as a mixed xanthine oxidase (XO) inhibitor with an IC50 value of 19.33 ± 0.45 μM. The promotion of reduced XO and the inhibition of the formation of uric acid by ECG led to a decrease in O2− radical. The stable ECG–XO complex was formed by hydrogen bonds and van der Waals forces, with the binding constant of the magnitude of 104 L mol−1, and ECG influenced the stability of the polypeptide skeleton and resulted in a more compact conformation of XO. Computational simulations further characterized the binding characteristics and revealed that the inhibitory mechanism of ECG on XO was likely that ECG bound to the vicinity of flavin adenine dinucleotide (FAD) and altered the conformation of XO, hindering the entry of substrate and the diffusion of catalytic products. ECG and allopurinol bound to different active sites of XO and exerted a synergistic inhibitory effect through enhancing their binding stability with XO and changing the target amino acid residues of XO. These findings may provide a theoretical basis for the further application of ECG in the fields of food nutrition and functional foods.

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Recent advances in the effect of ultrasound on the binding of protein−polyphenol complexes in foodstuff

et al. 2023

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Foodstuff is a complex system that consists of a variety of nutrients. Protein is the basis of human life and health, which is made up of amino acids combined in different proportional orders. Polyphenols are a class of small molecule active substances with strong pro‐life health effects. It has been found that protein and polyphenols can be combined by covalent and non‐covalent interactions to form complex delivery carriers. The interaction between the two can effectively improve the physiological activities of proteins and enhance the bio‐accessibility of polyphenols. With the maturation of ultrasound technology, several studies have shown that ultrasound can promote the production of protein−polyphenol complexes. To promote the study of protein–polyphenol interactions in foodstuff by ultrasound technology, the preparation methods of protein−polyphenol complexes, the effects of ultrasound on complex generation, and analytical methods were systematically summarized based on an extensive literature review, and further research directions were proposed. It provides the reference for the ultrasound study of protein−polyphenol complexes.

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Interaction of eugenol with xanthine oxidase: Multi spectroscopic and in silico modelling approach

Cited by 12 publications

References 27 publications

Study on the interaction mechanism between luteoloside and xanthine oxidase by multi‐spectroscopic and molecular docking methods

Study on the interaction mechanism between luteoloside and xanthine oxidase by multi‐spectroscopic and molecular docking methods

Epicatechin Gallate as Xanthine Oxidase Inhibitor: Inhibitory Kinetics, Binding Characteristics, Synergistic Inhibition, and Action Mechanism

Recent advances in the effect of ultrasound on the binding of protein−polyphenol complexes in foodstuff

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