GM1 Ganglioside Inhibits β-Amyloid Oligomerization Induced by Sphingomyelin
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F16%3A00461881" target="_blank" >RIV/61388955:_____/16:00461881 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/anie.201603178" target="_blank" >http://dx.doi.org/10.1002/anie.201603178</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/anie.201603178" target="_blank" >10.1002/anie.201603178</a>
Alternative languages
Result language
angličtina
Original language name
GM1 Ganglioside Inhibits β-Amyloid Oligomerization Induced by Sphingomyelin
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Controlling structure and function of biomolecules at the molecular scale: theory meets experiment</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Angewandte Chemie - International Edition
ISSN
1433-7851
e-ISSN
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Volume of the periodical
55
Issue of the periodical within the volume
32
Country of publishing house
DE - GERMANY
Number of pages
5
Pages from-to
9411-9415
UT code for WoS article
000383371800055
EID of the result in the Scopus database
2-s2.0-84977486670