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Tetrameric Aβ40 and Aβ42 β-Barrel Structures by Extensive Atomistic Simulations. II. In Aqueous Solution

dc.rights.licenseopenen_US
dc.relation.isnodoublebab56607-eaca-409e-9a5c-4935f0eeb927*
dc.contributor.authorNGUYEN, Phuong.Hoang
dc.contributor.authorCAMPANERA, Josep Maria
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.accessioned2019
dc.date.available2019
dc.date.issued2019
dc.identifier.issn1520-6106en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/3808
dc.description.abstractEnAlzheimer’s disease (AD) is characterized by the accumulation of extracellular Aβ42 and Aβ40 oligomers and plaques. In a recent computational study, we found that the presence of the residues I41 and A42 increases significantly the propensity of Aβ to form a tetrameric β-barrel structure in a bilayer mimicking a neuronal membrane. In this work, we have determined the propensity of the two Aβ proteins to form tetrameric β-barrel structures in aqueous solution using four atomistic protein fields, that is Amber99SB-ILDN/TIP3P, OPLS/TIP3P, CHARMM36m/TIP3P-modified and Amber99SB/DISP. Extensive replica exchange molecular dynamics simulations make it clear that a β-barrel, made of two distinct β-hairpin motifs and an asymmetric arrangement of eight anti-parallel β-strands with an inner pore diameter of 0.7 nm, exists transiently for Aβ42 peptide, but this is less the case for Aβ40 peptide, due to the change of the CHC-CHC and the Cter-Cter interfaces. This study has several implications in AD.
dc.description.sponsorshipDynamique des membranes transductrices d'énergie : biogénèse et organisation supramoléculaire. - ANR-11-LABX-0011en_US
dc.description.sponsorshipCentre d'analyse de systèmes complexes dans les environnements complexes - 11-EQPX-0008en_US
dc.language.isoENen_US
dc.title.enTetrameric Aβ40 and Aβ42 β-Barrel Structures by Extensive Atomistic Simulations. II. In Aqueous Solution
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/acs.jpcb.9b05288
dc.subject.halChimie/Matériauxen_US
bordeaux.journalJournal of the Chemical Society B: Physical Organic Journal of the Chemical Society B: Physical Organicen_US
bordeaux.page3643-3648en_US
bordeaux.volume123en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.issue17en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03181379
hal.version1
hal.date.transferred2021-03-25T14:39:50Z
hal.exporttrue
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