dc.contributor.author | Vaaland, Ingrid Caroline | |
dc.contributor.author | Lopez, Oscar | |
dc.contributor.author | Puerta, Adrian | |
dc.contributor.author | Fernandes, Miguel X. | |
dc.contributor.author | Padron, Jose M. | |
dc.contributor.author | Fernandez-Bolanos, Jose G. | |
dc.contributor.author | Sydnes, Magne Olav | |
dc.contributor.author | Lindback, Emil | |
dc.date.accessioned | 2023-10-18T06:35:07Z | |
dc.date.available | 2023-10-18T06:35:07Z | |
dc.date.created | 2022-12-03T10:26:48Z | |
dc.date.issued | 2023-09 | |
dc.identifier.citation | Vaaland, I.C., Lopéz, O., Puerta, A., Fernandes, M.X., Padrón, J.M., Fernandez-Bolanos, J.G., Sydnes, M.O. & 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. | en_US |
dc.identifier.issn | 1475-6366 | |
dc.identifier.uri | https://hdl.handle.net/11250/3097151 | |
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. | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Informa UK Limited, trading as Taylor & Francis Group | en_US |
dc.rights | Navngivelse 4.0 Internasjonal | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/deed.no | * |
dc.subject | Alzheimer | en_US |
dc.subject | medisinsk kjemi | en_US |
dc.title | Investigation of the enantioselectivity of acetylcholinesterase and butyrylcholinesterase upon inhibition by tacrine-iminosugar heterodimers | en_US |
dc.type | Peer reviewed | en_US |
dc.type | Journal article | en_US |
dc.description.version | publishedVersion | en_US |
dc.rights.holder | © 2022 The Author(s). | en_US |
dc.subject.nsi | VDP::Matematikk og Naturvitenskap: 400::Kjemi: 440 | en_US |
dc.subject.nsi | VDP::Medisinske Fag: 700::Klinisk medisinske fag: 750::Nevrologi: 752 | en_US |
dc.source.pagenumber | 349-360 | en_US |
dc.source.volume | 38 | en_US |
dc.source.journal | Journal of Enzyme Inhibition and Medicinal Chemistry | en_US |
dc.source.issue | 1 | en_US |
dc.identifier.doi | 10.1080/14756366.2022.2150762 | |
dc.identifier.cristin | 2088117 | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |