dc.creator | Vaaland, I. Caroline | es |
dc.creator | López López, Óscar | es |
dc.creator | Puerta, Adrián | es |
dc.creator | Fernandes, Miguel X. | es |
dc.creator | Padrón, José M. | es |
dc.creator | Fernández-Bolaños Guzmán, José María | es |
dc.creator | Sydnes, Magne O. | es |
dc.creator | Lindback, Emil | es |
dc.date.accessioned | 2023-09-11T14:34:52Z | |
dc.date.available | 2023-09-11T14:34:52Z | |
dc.date.issued | 2023 | |
dc.identifier.citation | Vaaland, 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.issn | 1475-6366 | es |
dc.identifier.issn | 1475-6374 | es |
dc.identifier.uri | https://hdl.handle.net/11441/148866 | |
dc.description.abstract | The 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.sponsorship | Gobierno de España PID2020-116460RB-I00, PID2021-123059OB-I00 | es |
dc.description.sponsorship | European Commission. Fondo Social Europeo TESIS2020010055 | es |
dc.format | application/pdf | es |
dc.format.extent | 12 p. | es |
dc.language.iso | eng | es |
dc.publisher | Taylor & Francis | es |
dc.relation.ispartof | Journal of Enzyme Inhibition and Medicinal Chemistry, 38 (1), 349-360. | |
dc.rights | Atribución 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | Alzheimer’s disease | es |
dc.subject | Cholinesterases | es |
dc.subject | Enantiomers | es |
dc.subject | Inhibitors | es |
dc.subject | Modelling | es |
dc.title | Investigation of the Enantioselectivity of Acetylcholinesterase and Butyrylcholinesterase upon Inhibition by Tacrine-iminosugar Heterodimers | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Química orgánica | es |
dc.relation.projectID | PID2020-116460RB-I00 | es |
dc.relation.projectID | PID2021-123059OB-I00 | es |
dc.relation.projectID | TESIS2020010055 | es |
dc.relation.publisherversion | https://doi.org/10.1080/14756366.2022.2150762 | es |
dc.identifier.doi | 10.1080/14756366.2022.2150762 | es |
dc.journaltitle | Journal of Enzyme Inhibition and Medicinal Chemistry | es |
dc.publication.volumen | 38 | es |
dc.publication.issue | 1 | es |
dc.publication.initialPage | 349 | es |
dc.publication.endPage | 360 | es |
dc.contributor.funder | Gobierno de España | es |
dc.contributor.funder | European Commission. Fondo Social Europeo (FSO) | es |