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dc.rights.licenseopenen_US
dc.relation.isnodouble1f2595cc-9893-405b-bb5e-6c2c58c63d5c*
dc.contributor.authorNGUYEN, Phuong H.
dc.contributor.authorCAMPANERA, Josep M.
dc.contributor.authorNGO, Son Tung
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorDERREUMAUX, Philippe
dc.date.accessioned2020-05-11T10:46:14Z
dc.date.available2020-05-11T10:46:14Z
dc.date.issued2019
dc.identifier.issn1520-6106en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/7515
dc.description.abstractEnThe amyloid-beta (Abeta) 42 oligomers are much more toxic than Abeta40 oligomers in Alzheimer's disease. Numerous experiments indicate that toxicity could involve the formation of pores in membranes, but experimental high-resolution structure determination of these pore-forming Abeta oligomers has been impeded by aggregate heterogeneity. Using extensive atomistic simulations, low-resolution data obtained in lipid bilayers, and other theoretical factors, we proposed atomic structures of Abeta40 and Abeta42 beta-barrels in a bilayer mimicking a neuronal membrane. The 3D model, which consists of tetramer subunits, two distinct beta-hairpin motifs and an asymmetric arrangement of eight antiparallel beta-strands, is drastically destabilized for Abeta40 compared to its Abeta42 counterpart. Our computational modeling has several implications in Alzheimer's disease, sheds light on the amyloid pore hypothesis, and explains the higher deleterious property of Abeta42.
dc.language.isoENen_US
dc.subject.enVesicles
dc.subject.enPeptides and proteins
dc.subject.enOligomers
dc.subject.enMembranes
dc.subject.enChemical structure
dc.title.enTetrameric Abeta40 and Abeta42 beta-Barrel Structures by Extensive Atomistic Simulations. I. In a Bilayer Mimicking a Neuronal Membrane
dc.title.alternativeJ. Phys. Chem. Ben_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/acs.jpcb.9b01206
dc.subject.halChimie/Matériauxen_US
bordeaux.journalThe journal of physical chemistry. Ben_US
bordeaux.page3643-3648en_US
bordeaux.volume123en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue17en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03184037
hal.version1
hal.date.transferred2021-03-29T08:55:37Z
hal.exporttrue
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