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Interaction of abeta1-42 amyloids with lipids promotes "off-pathway" oligomerization and membrane damage

hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHENRY, Sarah
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorVIGNAUD, Helene
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorBOBO, Claude
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDECOSSAS, Marion
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorLAMBERT, Oliver
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHARTE, Etienne
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorALVES, Isabel
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorCULLIN, Christophe
ORCID: 0000-0003-4110-4677
IDREF: 85920959
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
dc.date.accessioned2020-09-03T08:02:09Z
dc.date.available2020-09-03T08:02:09Z
dc.date.issued2015
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10975
dc.description.abstractEnThe toxicity of amyloids, as Abeta1-42 involved in Alzheimer disease, is a subject under intense scrutiny. Many studies link their toxicity to the existence of various intermediate structures prior to fiber formation and/or their specific interaction with membranes. In this study we focused on the interaction between membrane models and Abeta1-42 peptides and variants (L34T, mG37C) produced in E. coli and purified in monomeric form. We evaluated the interaction of a toxic stable oligomeric form (oG37C) with membranes as comparison. Using various biophysical techniques as fluorescence and plasmon waveguide resonance, we clearly established that the oG37C interacts strongly with membranes leading to its disruption. All the studied peptides destabilized liposomes and accumulated slowly on the membrane (rate constant 0.02 min(-1)). Only the oG37C exhibited a particular pattern of interaction, comprising two steps: the initial binding followed by membrane reorganization. Cryo-TEM was used to visualize the peptide effect on liposome morphologies. Both oG37C and mG37C lead to PG membrane fragmentation. The PG membrane promotes peptide oligomerization, implicated in membrane disruption. WT (Abeta1-42) also perturbs liposome organization with membrane deformation rather than disruption. For all the peptides studied, their interaction with the membranes changes their fibrillization process, with less fibers and more small aggregates being formed. These studies allowed to establish, a correlation between toxicity, fiber formation, and membrane disruption.
dc.language.isoen
dc.title.enInteraction of abeta1-42 amyloids with lipids promotes "off-pathway" oligomerization and membrane damage
dc.typeArticle de revue
dc.identifier.doi10.1021/bm501837w
dc.subject.halChimie/Matériaux
bordeaux.journalBiomacromolecules
bordeaux.page944-50
bordeaux.volume16
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue3
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biomacromolecules&rft.date=2015&rft.volume=16&rft.issue=3&rft.spage=944-50&rft.epage=944-50&rft.au=HENRY,%20Sarah&VIGNAUD,%20Helene&BOBO,%20Claude&DECOSSAS,%20Marion&LAMBERT,%20Oliver&rft.genre=article


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