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dc.rights.licenseopenen_US
dc.contributor.authorSMERALDA, Willy
dc.contributor.authorSINCE, Marc
dc.contributor.authorCORVAISIER, Sophie
dc.contributor.authorFAYOLL, Dimitri
dc.contributor.authorCARDIN, Julien
dc.contributor.authorDUPREY, Sylvain
dc.contributor.authorJOURDAN, Jean-Pierre
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCULLIN, Christophe
ORCID: 0000-0003-4110-4677
IDREF: 85920959
dc.contributor.authorMALZERT-FREON, Aurelie
dc.date.accessioned2024-04-18T08:16:16Z
dc.date.available2024-04-18T08:16:16Z
dc.date.issued2023-11-30
dc.identifier.issn1661-6596en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199216
dc.description.abstractEnAlzheimer's disease (AD) is the most widespread form of senile dementia worldwide and represents a leading socioeconomic problem in healthcare. Although it is widely debated, the aggregation of the amyloid β peptide (Aβ) is linked to the onset and progression of this neurodegenerative disease. Molecules capable of interfering with specific steps in the fibrillation process remain of pharmacological interest. To identify such compounds, we have set up a small molecule screening process combining multiple experimental methods (UV and florescence spectrometry, ITC, and ATR-FTIR) to identify and characterise potential modulators of Aβ 1-42 fibrillation through the description of the biochemical interactions (molecule-membrane Aβ peptide). Three known modulators, namely bexarotene, Chicago sky blue and indomethacin, have been evaluated through this process, and their modulation mechanism in the presence of a biomembrane has been described. Such a well-adapted physico-chemical approach to drug discovery proves to be an undeniable asset for the rapid characterisation of compounds of therapeutic interest for Alzheimer's disease. This strategy could be adapted and transposed to search for modulators of other amyloids such as tau protein.
dc.language.isoENen_US
dc.subject.enAlzheimer’s disease
dc.subject.enliposomes
dc.subject.enβ-amyloïd
dc.subject.endrug discovery
dc.subject.enbexarotene
dc.subject.enindomethacin
dc.subject.enChicago sky blue
dc.title.enA biomimetic multiparametric assay to characterise anti-amyloid drugs
dc.typeArticle de revueen_US
dc.identifier.doi10.3390/ijms242316982en_US
dc.subject.halSciences du Vivant [q-bio]/Sciences pharmaceutiquesen_US
dc.subject.halSciences de l'ingénieur [physics]en_US
bordeaux.journalInternational Journal of Molecular Sciencesen_US
bordeaux.page16982en_US
bordeaux.volume24en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue23en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-04315267
hal.version1
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=International%20Journal%20of%20Molecular%20Sciences&rft.date=2023-11-30&rft.volume=24&rft.issue=23&rft.spage=16982&rft.epage=16982&rft.eissn=1661-6596&rft.issn=1661-6596&rft.au=SMERALDA,%20Willy&SINCE,%20Marc&CORVAISIER,%20Sophie&FAYOLL,%20Dimitri&CARDIN,%20Julien&rft.genre=article


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