In vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase

Vista sencilla de ítem
dc.contributor.authorSierra, Karina
dc.contributor.authorde Andrade, Jean Paulo
dc.contributor.authorR. Tallini, Luciana
dc.contributor.authorOsorio, Edison H.
dc.contributor.authorYañéz, Osvaldo
dc.contributor.authorOsorio, Manuel Isaías
dc.contributor.authorOleas, Nora H.
dc.contributor.authorGarcía-Beltrán, Olimpo
dc.contributor.authorde S. Borges, Warley
dc.contributor.authorBastida, Jaume
dc.contributor.authorOsorio, Edison
dc.contributor.authorCortes, Natalie
dc.date.accessioned2024-05-07T16:11:50Z
dc.date.available2024-05-07T16:11:50Z
dc.date.issued2022-06
dc.descriptionIndexación: Scopus.
dc.description.abstractZephyranthes 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. © 2022 The Authors
dc.description.urihttps://www-sciencedirect-com.recursosbiblioteca.unab.cl/science/article/pii/S075333222200405X?via%3Dihub
dc.identifier.citationBiomedicine and Pharmacotherapy, Volume 150, June 2022, Article number 113016
dc.identifier.doi10.1016/j.biopha.2022.113016
dc.identifier.issn0753-3322
dc.identifier.urihttps://repositorio.unab.cl/handle/ria/56608
dc.language.isoen
dc.publisherElsevier Masson s.r.l.
dc.rights.licenseCC BY 4.0 DEED Atribución 4.0 Internacional
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/deed.es
dc.subjectAcetylcholinesterase inhibition
dc.subjectAmaryllidaceae alkaloids
dc.subjectGalanthine
dc.subjectMolecular docking
dc.subjectMolecular dynamics
dc.titleIn vitro and in silico analysis of galanthine from Zephyranthes carinata as an inhibitor of acetylcholinesterase
dc.typeArtículo
Archivos
Bloque original
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
Sierra_In_vitro_and_in_silico.pdf
Tamaño:
3.21 MB
Formato:
Adobe Portable Document Format
Descripción:
TEXTO COMPLETO EN INGLÉS
Descargar
Bloque de licencias
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
license.txt
Tamaño:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descripción:
Descargar
Colecciones
Fac.CV - Artículos de Revista