Screening for selective inhibitors of xanthine oxidase from Flos Chrysanthemum using ultrafiltration LC–MS combined with enzyme channel blocking

Song, Hui‐Peng; Zhang, Hui; Fu, Yu; Mo, Hua-yan; Zhang, Mu; Chen, Jun; Li, Ping

doi:10.1016/j.jchromb.2014.05.001

Cited by 86 publications

(51 citation statements)

References 19 publications

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“…In addition, the complex isolation procedures may lead to the missing of minor or unstable components. Thus, simple, timesaving and comprehensive methods for activity screening from complex mixtures have attracted increasingly attention [17,18].…”

Section: Introductionmentioning

confidence: 99%

Screening of direct thrombin inhibitors from Radix Salviae Miltiorrhizae by a peak fractionation approach

Song

et al. 2015

Journal of Pharmaceutical and Biomedical Analysis

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Section: Introductionmentioning

confidence: 99%

Screening of direct thrombin inhibitors from Radix Salviae Miltiorrhizae by a peak fractionation approach

Song

et al. 2015

Journal of Pharmaceutical and Biomedical Analysis

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“…[35][36][37] The present study showed that, aer 24 h metabolism, the phase-I metabolites (such as A1/A2/A3) were detected in the solution sample of zebrash. In subsequent phase-II reactions, these activated xenobiotic metabolites are prone to be conjugated with charged species such as glutathione (GSH), sulfate, glycine, or glucuronic acid.…”

Section: -34mentioning

confidence: 86%

Metabolism of five diterpenoid lactones from Dioscorea bulbifera tubers in zebrafish

et al. 2018

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Diterpenoid lactones (DLs) have been reported to be the main hepatotoxic constituents in Dioscorea bulbifera tubers (DBT), a traditional Chinese medicinal herb. The acquisition of early information regarding its metabolism is critical for evaluating the potential hepatotoxicity of DLs. We investigated, for the first time, the main metabolites of diosbulbin A (DIOA), diosbulbin C (DIOC), diosbulbin (DIOG), diosbulbin (DIOM) and diosbulbin (DIOF) in adult zebrafish. By using ultra-high performance liquid chromatographyquadrupole time-of-flight mass spectrometry (UHPLC-QTOF MS), 6, 2, 7, 5 and 4 metabolites of DIOA, DIOC, DIOF, DIOM and DIOG were identified in the zebrafish body and the aqueous solution, respectively.Both phase-I and phase-II metabolites were observed in the metabolic profiles and the metabolic pathways involved in hydroxyl reduction, glucuronidation, glutathione conjugation and sulfation. The above results indicated that hepatocytic metabolism might be the major route of clearance for DLs. This study provided important information for the understanding of the metabolism of DLs in DBT.

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“…The method so developed can differentiate potential inhibitors binding to the active site of the enzyme and on the allosteric site that could displace febuxostat. Utilizing the method, authors isolated and screened four bioactive constituents as XO inhibitor from Flos chrysanthemum …”

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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Screening for selective inhibitors of xanthine oxidase from Flos Chrysanthemum using ultrafiltration LC–MS combined with enzyme channel blocking

Cited by 86 publications

References 19 publications

Screening of direct thrombin inhibitors from Radix Salviae Miltiorrhizae by a peak fractionation approach

Screening of direct thrombin inhibitors from Radix Salviae Miltiorrhizae by a peak fractionation approach

Metabolism of five diterpenoid lactones from Dioscorea bulbifera tubers in zebrafish

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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