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dc.creatorVaaland, I. Carolinees
dc.creatorLópez López, Óscares
dc.creatorPuerta, Adriánes
dc.creatorFernandes, Miguel X.es
dc.creatorPadrón, José M.es
dc.creatorFernández-Bolaños Guzmán, José Maríaes
dc.creatorSydnes, Magne O.es
dc.creatorLindback, Emiles
dc.date.accessioned2023-09-11T14:34:52Z
dc.date.available2023-09-11T14:34:52Z
dc.date.issued2023
dc.identifier.citationVaaland, I.C., López López, Ó., Puerta, A., Fernandes, M.X., Padrón, J.M., Fernández-Bolaños Guzmán, J.M.,...,Lindback, E. (2023). Investigation of the Enantioselectivity of Acetylcholinesterase and Butyrylcholinesterase upon Inhibition by Tacrine-iminosugar Heterodimers. Journal of Enzyme Inhibition and Medicinal Chemistry, 38 (1), 349-360. https://doi.org/10.1080/14756366.2022.2150762.
dc.identifier.issn1475-6366es
dc.identifier.issn1475-6374es
dc.identifier.urihttps://hdl.handle.net/11441/148866
dc.description.abstractThe copper-catalysed azide-alkyne cycloaddition was applied to prepare three enantiomeric pairs of heterodimers containing a tacrine residue and a 1,4-dideoxy-1,4-imino-D-arabinitol (DAB) or 1,4-dideoxy-1,4-imino-L-arabinitol (LAB) moiety held together via linkers of variable lengths containing a 1,2,3-triazole ring and 3, 4, or 7 CH2 groups. The heterodimers were tested as inhibitors of butyrylcholinesterase (BuChE) and acetylcholinesterase (AChE). The enantiomeric heterodimers with the longest linkers exhibited the highest inhibition potencies for AChE (IC50 = 9.7 nM and 11 nM) and BuChE (IC50 = 8.1 nM and 9.1 nM). AChE exhibited the highest enantioselectivity (ca. 4-fold). The enantiomeric pairs of the heterodimers were found to be inactive (GI50 > 100 µM), or to have weak antiproliferative properties (GI50 = 84–97 µM) against a panel of human cancer cells.es
dc.description.sponsorshipGobierno de España PID2020-116460RB-I00, PID2021-123059OB-I00es
dc.description.sponsorshipEuropean Commission. Fondo Social Europeo TESIS2020010055es
dc.formatapplication/pdfes
dc.format.extent12 p.es
dc.language.isoenges
dc.publisherTaylor & Francises
dc.relation.ispartofJournal of Enzyme Inhibition and Medicinal Chemistry, 38 (1), 349-360.
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectAlzheimer’s diseasees
dc.subjectCholinesteraseses
dc.subjectEnantiomerses
dc.subjectInhibitorses
dc.subjectModellinges
dc.titleInvestigation of the Enantioselectivity of Acetylcholinesterase and Butyrylcholinesterase upon Inhibition by Tacrine-iminosugar Heterodimerses
dc.typeinfo:eu-repo/semantics/articlees
dcterms.identifierhttps://ror.org/03yxnpp24
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Química orgánicaes
dc.relation.projectIDPID2020-116460RB-I00es
dc.relation.projectIDPID2021-123059OB-I00es
dc.relation.projectIDTESIS2020010055es
dc.relation.publisherversionhttps://doi.org/10.1080/14756366.2022.2150762es
dc.identifier.doi10.1080/14756366.2022.2150762es
dc.journaltitleJournal of Enzyme Inhibition and Medicinal Chemistryes
dc.publication.volumen38es
dc.publication.issue1es
dc.publication.initialPage349es
dc.publication.endPage360es
dc.contributor.funderGobierno de Españaes
dc.contributor.funderEuropean Commission. Fondo Social Europeo (FSO)es

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Except where otherwise noted, this item's license is described as: Atribución 4.0 Internacional