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dc.contributor.authorAutorSierra, Karina
dc.contributor.authorAutorAndrade, Jean Paulo de
dc.contributor.authorAutorTallini, Luciana R.
dc.contributor.authorAutorOsorio, Edison H.
dc.contributor.authorAutorYáñez, Osvaldo
dc.contributor.authorAutorOsorio, Manuel Isaías
dc.contributor.authorAutorOleas, Nora H.
dc.contributor.authorAutorGarcía-Beltrán, Olimpo
dc.contributor.authorAutorBorges, Warley de S.
dc.contributor.authorAutorBastida, Jaume
dc.contributor.authorAutorOsorio, Edison
dc.contributor.authorAutorCortes, Natalie
dc.contributor.otherCarreraFacultad de ingeniería y negocioses
dc.date.accessionedFecha ingreso2022-05-16T18:02:40Z
dc.date.availableFecha disponible2022-05-16T18:02:40Z
dc.date.issuedFecha publicación2022-04-25
dc.identifier.citationReferencia BibliográficaBiomedicine & Pharmacotherapy 150, 9 p.
dc.identifier.issnISSN0753-3322
dc.identifier.uriURLhttp://repositorio.udla.cl/xmlui/handle/udla/996
dc.identifier.uriURLhttps://www.sciencedirect.com/science/article/pii/S075333222200405X?via%3Dihub
dc.description.abstractResumenZephyranthes carinata Herb., a specie of the Amaryllidoideae subfamily, has been reported to have inhibitory activity against acetylcholinesterase. However, scientific evidence related to their bioactive alkaloids has been lacking. Thus, this study describes the isolation of the alkaloids of this plant, and their inhibition of the enzymes acetylcholinesterase (eeAChE) and butyrylcholinesterase (eqBuChE), being galanthine the main component. Additionally, haemanthamine, hamayne, lycoramine, lycorine, tazettine, trisphaeridine and vittatine/crinine were also isolated. The results showed that galanthine has significant activity at low micromolar concentrations for eeAChE (IC50 = 1.96 μg/mL). The in-silico study allowed to establish at a molecular level the high affinity and the way galanthine interacts with the active site of the TcAChE enzyme, information that corroborates the result of the experimental IC50. However, according to molecular dynamics (MD) analysis, it is also suggested that galanthine presents a different inhibition mode that the one observed for galanthamine, by presenting interaction with peripheral anionic binding site of the enzyme, which prevents the entrance and exit of molecules from the active site. Thus, in vitro screening assays plus rapid computer development play an essential role in the search for new cholinesterase inhibitors by identifying unknown bio-interactions between bioactive compounds and biological targets.es
dc.format.extentdc.format.extent9 páginas
dc.format.extentdc.format.extent3.211Mb
dc.format.mimetypedc.format.mimetypePDF
dc.language.isoLenguaje ISOen
dc.publisherEditorElsevier
dc.sourceFuentesBiomedicine & Pharmacotherapy
dc.subjectPalabras ClavesAcetylcholinesterase inhibitiones
dc.subjectPalabras ClavesGalanthinees
dc.subjectPalabras ClavesAmaryllidaceae alkaloidses
dc.subjectPalabras ClavesMolecular dockinges
dc.subjectPalabras ClavesMolecular dinamicses
dc.titleTítuloIn vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterasees
dc.typeTipo de DocumentoArtículoes
dc.udla.catalogadordc.udla.catalogadorCBM
dc.udla.indexdc.udla.indexSCOPUS
dc.identifier.doidc.identifier.doihttps://doi.org/10.1016/j.biopha.2022.113016
dc.udla.privacidaddc.udla.privacidadDocumento públicoes


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