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1000 Titel
  • An innovative cell model revealed the inhibitory effect of flavanone structure on peroxynitrite production through interaction with the IKKβ kinase domain at ATP binding site
1000 Autor/in
  1. Charoensin, Supochana |
  2. Huang, Tzou-Chi |
  3. Hsu, Jue-Liang |
1000 Erscheinungsjahr 2020
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2020-04-27
1000 Erschienen in
1000 Quellenangabe
  • 8(6):2904-2912
1000 Copyrightjahr
  • 2020
1000 Lizenz
1000 Verlagsversion
  • https://doi.org/10.1002/fsn3.1591 |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • It is hypothesized that the oxidative/nitrosative stress inhibitory effect of a flavanone is governed by its chemical structure. However, the existing cell-based antioxidant assays primarily focus on single chemical to initiate toxic species production. In this study, a novel cell model using macrophage treated with a combination of PMA and LPS leading to generation of peroxynitrite was proposed to provide a more real physiological condition. Three flavanones (eriodictyol, naringenin, and pinocembrin) with different number of ortho-dihydroxyl groups on B-ring were used to provide a more comprehensive evaluation of the role of chemical structure in the new model. Dihydrorhodamine123 assay, protein immunoblotting, immunofluorescence assay, and in silico analysis by molecular docking between the flavanones and IKKβ catalytic kinase domain at the ATP binding site were employed. Results indicated that the generation of peroxynitrite was decreased at 10 µM of flavanones; eriodictyol was the most effective inhibitor. Western blot analysis and confocal fluorescence image also showed that eriodictyol could inhibit iNOS and p47 protein expressions through the inhibition of NF-kB translocation and performed the maximal inhibition compared to that of the other groups. In addition, the highest CDOCKER energy values of eriodictyol (38.6703 kcal/mol) confirmed that the 3′,4′-ortho-dihydroxylation on the B-ring played a crucial role in binding with IKKβ kinase domain at ATP binding site. Finally, we propose that the ortho-dihydroxyl groups on B-ring of flavanone may influence directly the occupation of the ATP binding site of IKKβ kinase domain leading to the abrogation of peroxynitrite formation in the innovative cell model.
1000 Sacherschließung
lokal cell model
lokal chemical structure
lokal flavanone
lokal antioxidant activity
lokal peroxynitrite
lokal macrophage
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://orcid.org/0000-0003-1314-0240|https://frl.publisso.de/adhoc/uri/SHVhbmcsIFR6b3UtQ2hp|https://orcid.org/0000-0002-6771-6690
1000 Label
1000 Förderer
  1. Taiwan ICDF |
  2. Ministry of Science and Technology, Taiwan |
1000 Fördernummer
  1. -
  2. MOST108-2113-M-020-001
1000 Förderprogramm
  1. -
  2. -
1000 Dateien
1000 Förderung
  1. 1000 joinedFunding-child
    1000 Förderer Taiwan ICDF |
    1000 Förderprogramm -
    1000 Fördernummer -
  2. 1000 joinedFunding-child
    1000 Förderer Ministry of Science and Technology, Taiwan |
    1000 Förderprogramm -
    1000 Fördernummer MOST108-2113-M-020-001
1000 Objektart article
1000 Beschrieben durch
1000 @id frl:6430610.rdf
1000 Erstellt am 2021-12-08T11:54:20.679+0100
1000 Erstellt von 286
1000 beschreibt frl:6430610
1000 Bearbeitet von 286
1000 Zuletzt bearbeitet Wed Dec 08 11:55:40 CET 2021
1000 Objekt bearb. Wed Dec 08 11:55:16 CET 2021
1000 Vgl. frl:6430610
1000 Oai Id
  1. oai:frl.publisso.de:frl:6430610 |
1000 Sichtbarkeit Metadaten public
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