Development of a method to screen and isolate potential xanthine oxidase inhibitors from Panax japlcus var via ultrafiltration liquid chromatography combined with counter-current chromatography

Li, Sainan; Tang, Ying; Liu, Chunming; Li, Jing; Guo, Liping; Zhang, Yuchi

doi:10.1016/j.talanta.2014.12.005

Cited by 49 publications

(27 citation statements)

References 25 publications

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“…High concentrations of uric acid in the blood are linked to gout , and XOD is believed to contribute to gout‐related diseases , and is also responsible for oxidative damage to tissues in the body . XOD inhibitors such as allopurinol are reported to be an effective treatment for gout because they decrease the production of uric acid , but side effects can include fever, skin rashes, and renal failure . Natural product XOD inhibitors are therefore potential drug candidates because they may induce less severe side effects .…”

Section: Introductionmentioning

confidence: 99%

Screening inhibitors of xanthine oxidase from natural products using enzyme immobilized magnetic beads by high‐performance liquid chromatography coupled with tandem mass spectrometry

Wang

et al. 2017

J of Separation Science

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In this study, high-performance liquid chromatography coupled with tandem mass spectrometry was used to assess the results of bioactive compound screening from natural products using immobilized enzyme magnetic beads. We compared three commercial magnetic beads with modified amino, carboxy, and N-hydroxysuccinimide groups, respectively. Amino magnetic beads performed best for immobilization and were selected for further experiments. Xanthine oxidase was immobilized on amino magnetic beads and applied to screen potential inhibitors in fresh Zingiber officinale Roscoe, extracts of Scutellaria baicalensis Georgi, and Pueraria lobata Ohwi. In total, 12 potential xanthine oxidase ligands were identified from fresh Zingiber root and Scutellaria root extracts, of which eight were characterized and the concentration required for 50% inhibition was determined. Preliminary structure-function relationships were discussed based on these results. A convenient and effective method was therefore developed for the identification of active compounds from complex natural product mixtures.

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Section: Introductionmentioning

confidence: 99%

Screening inhibitors of xanthine oxidase from natural products using enzyme immobilized magnetic beads by high‐performance liquid chromatography coupled with tandem mass spectrometry

Wang

et al. 2017

J of Separation Science

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“…Several methods for the separation and analysis of CHS‐IVa in raw herbs have been reported, including high‐performance liquid chromatography (HPLC), liquid chromatography combined with counter‐current chromatography, HPLC with diode array–evaporative light scattering detectors and mass spectrometry, liquid chromatography with electrospray ionization quadrupole time‐of‐flight tandem mass spectrometry or ultra‐performance liquid chromatography with photodiode array detector and electrospray ionization/mass spectrometry (Li et al , ; Ha et al , ; Xie et al , ; Song et al , ). However, none of these methods have been used for pharmacokinetic studies.…”

Section: Introductionmentioning

confidence: 99%

Determination and validation of chikusetsusaponin IVa in rat plasma by UPLC‐MS/MS and its application to pharmacokinetic study

Wang

Liu

Guo

et al. 2016

Biomedical Chromatography

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A novel, sensitive and rapid ultra-performance liquid chromatography-tandem mass spectrometric method for the quantification of chikusetsusaponin IVa (CHS-IVa) in rat plasma was established and validated. Plasma samples were pre-treated by precipitation of protein with acetonitrile and chromatographed on a Waters Symmetry C18 analytical column (4.6 × 50 mm, i.d., 3.5 μm) using a mobile phase consisting of methanol and water containing 0.05% formic acid (55:45, v/v) at a flow rate of 0.4 mL/min. The deprotonated molecular ions [M - H](-) were employed in electrospray negative ionization mode and selected reaction monitoring transitions were performed for detection. The calibration curves exhibited good linearity (r > 0.99) over the range of 0.5-1000 ng/mL for CHS-IVa. The recoveries of CHS-IVa were >92.5% and exhibited no severe matrix effect. This method was successfully applied in the pharmacokinetic study of CHS-IVa in rats. For oral administration, the plasma concentrations of CHS-IVa increased to a peak value at 0.35 ± 0.14 h, followed by a gradual decrease to the lower limit of quantitation in 24 h. For intravenous administration, the plasma concentrations of CHS-IVa decreased quickly (t1/2 , 1.59 ± 0.25 h). The absolute bioavailability of CHS-IVa in rats was 8.63%. Copyright © 2016 John Wiley & Sons, Ltd.

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“…They mainly focused on the method based on ultrafiltration liquid chromatography–tandem mass spectrometry (UF‐LC–MS) in association with high‐speed countercurrent chromatography. Utilizing this technique, they isolated six potential XO inhibitors namely ( R )‐major side (IC 50 : 2.08 mg/mL), Chikusetsusaponin IVa (IC 50 : 5.03 mg/mL), oleanolic acid‐28‐ O ‐β‐D‐glucopyranoside (IC 50 : 3.52 mg/ml), notoginsenoside Fe (IC 50 : 4.20 mg/ml), ginsenoside Rb 2 (IC 50 : 2.71 mg/mL), and ginsenoside Rd (IC 50 : 1.86 mg/mL) from Panax japlcus in highest purity …”

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

101

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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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Development of a method to screen and isolate potential xanthine oxidase inhibitors from Panax japlcus var via ultrafiltration liquid chromatography combined with counter-current chromatography

Cited by 49 publications

References 25 publications

Screening inhibitors of xanthine oxidase from natural products using enzyme immobilized magnetic beads by high‐performance liquid chromatography coupled with tandem mass spectrometry

Screening inhibitors of xanthine oxidase from natural products using enzyme immobilized magnetic beads by high‐performance liquid chromatography coupled with tandem mass spectrometry

Determination and validation of chikusetsusaponin IVa in rat plasma by UPLC‐MS/MS and its application to pharmacokinetic study

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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