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dc.rights.licenseopenen_US
dc.contributor.authorSMERALDA, Willy
dc.contributor.authorSINCE, Marc
dc.contributor.authorCARDIN, Julien
dc.contributor.authorCORVAISIER, Sophie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
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.accessioned2021-07-07T14:36:37Z
dc.date.available2021-07-07T14:36:37Z
dc.date.issued2021
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/95019
dc.description.abstractEnAlzheimer's disease is the most common form of senile dementia in the world, and amyloid beta peptide1-42 (Abeta1-42) is one of its two principal biological hallmarks. While interactome concept was getting forward the scientific community, we proposed that the study of the molecular interactions of amyloid beta peptide with the biological membranes will allow to highlight underlying mechanisms responsive of AD. We have developed two simple liposomal formulations (phosphatidylcholine, cholesterol, phosphatidylglycerol) mimicking neuronal cell membrane (composition, charge, curvature radius). Interactions with Abeta1-42 and mutant oG37C, a stable oligomeric form of the peptide, were characterized according to a simple multiparametric procedure based on ThT fluorescence, liposome leakage assay, ATR-FTIR spectroscopy. Kinetic aggregation, membrane damage and peptide conformation provided our first methodologic bases to develop an original model to describe interactions of Abeta peptide and lipids.
dc.language.isoENen_US
dc.subject.enAlzheimer's disease
dc.subject.enLiposomes β-Amyloid
dc.subject.enMembranes
dc.title.enbeta-Amyloid peptide interactions with biomimetic membranes: A multiparametric characterization
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.ijbiomac.2021.03.107en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalInternational Journal of Biological Macromoleculesen_US
bordeaux.page769-777en_US
bordeaux.volume181en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03187852
hal.exportfalse
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