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GM1 Ganglioside Inhibits β-Amyloid Oligomerization Induced by Sphingomyelin
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SYSNO ASEP 0461881 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title GM1 Ganglioside Inhibits β-Amyloid Oligomerization Induced by Sphingomyelin Author(s) Amaro, Mariana (UFCH-W) RID, ORCID
Šachl, Radek (UFCH-W) RID, ORCID
Aydogan, Gokcan (UFCH-W)
Mikhalyov, I. (RU)
Vácha, R. (CZ)
Hof, Martin (UFCH-W) RID, ORCIDSource Title Angewandte Chemie - International Edition. - : Wiley - ISSN 1433-7851
Roč. 55, č. 32 (2016), s. 9411-9415Number of pages 5 s. Language eng - English Country DE - Germany Keywords amyloid beta-peptides ; Alzheimer's disease ; diffusion coefficients Subject RIV CF - Physical ; Theoretical Chemistry R&D Projects GBP208/12/G016 GA ČR - Czech Science Foundation (CSF) Institutional support UFCH-W - RVO:61388955 UT WOS 000383371800055 EID SCOPUS 84977486670 DOI 10.1002/anie.201603178 Annotation Beta-Amyloid (Aβ) oligomers are neurotoxic and implicated in Alzheimer's disease. Neuronal plasma membranes may mediate formation of Aβ oligomers in vivo. Membrane components sphingomyelin and GM1 have been shown to promote aggregation of Aβ; however, these studies were performed under extreme, non-physiological conditions. We demonstrate that physiological levels of GM1, organized in nanodomains do not seed oligomerization of Aβ40 monomers. We show that sphingomyelin triggers oligomerization of Aβ40 and that GM1 is counteractive thus preventing oligomerization. We propose a molecular explanation that is supported by all-atom molecular dynamics simulations. The preventive role of GM1 in the oligomerization of Aβ40 suggests that decreasing levels of GM1 in the brain, for example, due to aging, could reduce protection against Aβ oligomerization and contribute to the onset of Alzheimer's disease. Workplace J. Heyrovsky Institute of Physical Chemistry Contact Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Year of Publishing 2017
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