Flavonoids from Sideritis Species: Human Monoamine Oxidase (hMAO) Inhibitory Activities, Molecular Docking Studies and Crystal Structure of Xanthomicrol

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dc.contributor.authorTurkmenoglu, Fatma Pinar
dc.contributor.authorBaysal, Ipek
dc.contributor.authorCiftci-Yabanoglu, Samiye
dc.contributor.authorYelekci, Kemal
dc.contributor.authorTemel, Hamdi
dc.contributor.authorPasa, Salih
dc.contributor.authorEzer, Nurten
dc.date.accessioned2024-04-24T17:20:52Z
dc.date.available2024-04-24T17:20:52Z
dc.date.issued2015
dc.departmentDicle Üniversitesien_US
dc.description.abstractThe inhibitory effects of flavonoids on monoamine oxidases (MAOs) have attracted great interest since alterations in monoaminergic transmission are reported to be related to neurodegenerative diseases such as Parkinson's and Alzheimer's diseases and psychiatric disorders such as depression and anxiety, thus MAOs may be considered as targets for the treatment of these multi-factorial diseases. In the present study, four Sideritis flavonoids, xanthomicrol (1), isoscutellarein 7-O-[6'''-O-acetyl--d-allopyranosyl-(12)]--d-glucopyranoside (2), isoscutellarein 7-O-[6'''-O-acetyl--d-allopyranosyl-(12)]-6''-O-acetyl--d-glucopyranoside (3) and salvigenin (4) were docked computationally into the active site of the human monoamine oxidase isoforms (hMAO-A and hMAO-B) and were also investigated for their hMAO inhibitory potencies using recombinant hMAO isoenzymes. The flavonoids inhibited hMAO-A selectively and reversibly in a competitive mode. Salvigenin (4) was found to be the most potent hMAO-A inhibitor, while xanthomicrol (1) appeared as the most selective hMAO-A inhibitor. The computationally obtained results were in good agreement with the corresponding experimental values. In addition, the x-ray structure of xanthomicrol (1) has been shown. The current work warrants further preclinical studies to assess the potential of xanthomicrol (1) and salvigenin (4) as new selective and reversible hMAO-A inhibitors for the treatment of depression and anxiety.en_US
dc.description.sponsorshipHacettepe University Scientific Research Projects Coordination Unit [HUAF 02T10102001]en_US
dc.description.sponsorshipPresent work was supported by a grant from Hacettepe University Scientific Research Projects Coordination Unit (Project No: HUAF 02T10102001). The authors would like to thank Erhan Palaska (Hacettepe University, Faculty of Pharmacy, Department of Pharmaceutical Chemistry) for the ESI-MS spectra of the compounds reported in this study.en_US
dc.identifier.doi10.3390/molecules20057454
dc.identifier.endpage7473en_US
dc.identifier.issn1420-3049
dc.identifier.issue5en_US
dc.identifier.pmid25915461
dc.identifier.scopus2-s2.0-84929223384
dc.identifier.scopusqualityQ1
dc.identifier.startpage7454en_US
dc.identifier.urihttps://doi.org/10.3390/molecules20057454
dc.identifier.urihttps://hdl.handle.net/11468/19280
dc.identifier.volume20en_US
dc.identifier.wosWOS:000357157600002
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoenen_US
dc.publisherMdpien_US
dc.relation.ispartofMolecules
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectSideritisen_US
dc.subjectFlavonoiden_US
dc.subjectXanthomicrolen_US
dc.subjectSalvigeninen_US
dc.subjectMonoamine Oxidaseen_US
dc.subjectInhibitionen_US
dc.subjectMolecular Dockingen_US
dc.subjectX-Ray Diffraction Investigationen_US
dc.titleFlavonoids from Sideritis Species: Human Monoamine Oxidase (hMAO) Inhibitory Activities, Molecular Docking Studies and Crystal Structure of Xanthomicrolen_US
dc.titleFlavonoids from Sideritis Species: Human Monoamine Oxidase (hMAO) Inhibitory Activities, Molecular Docking Studies and Crystal Structure of Xanthomicrol
dc.typeArticleen_US

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