AMARO, Mariana, Radek ŠACHL, Gokcan AYDOGAN, Ilya I. MIKHALYOV, Robert VÁCHA and Martin HOF. (GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin. Angewandte Chemie International Edition. WEINHEIM: Wiley-V C H VERLAG GMBH, 2016, vol. 55, No 32, p. 9411-9415. ISSN 1433-7851. Available from: https://dx.doi.org/10.1002/anie.201603178.
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Basic information
Original name (GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin
Authors AMARO, Mariana (203 Czech Republic), Radek ŠACHL (203 Czech Republic), Gokcan AYDOGAN (203 Czech Republic), Ilya I. MIKHALYOV (643 Russian Federation), Robert VÁCHA (203 Czech Republic, guarantor, belonging to the institution) and Martin HOF (276 Germany).
Edition Angewandte Chemie International Edition, WEINHEIM, Wiley-V C H VERLAG GMBH, 2016, 1433-7851.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Germany
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 11.994
RIV identification code RIV/00216224:14740/16:00088531
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1002/anie.201603178
UT WoS 000383371800055
Keywords in English Alzheimer's disease; amyloid beta-peptides; diffusion coefficients; fluorescence spectroscopy; neuroprotectives
Tags rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 1/3/2017 13:59.
Abstract
beta-Amyloid (A beta) oligomers are neurotoxic and implicated in Alzheimer's disease. Neuronal plasma membranes may mediate formation of A beta oligomers in vivo. Membrane components sphingomyelin and GM(1) have been shown to promote aggregation of A beta; however, these studies were performed under extreme, non-physiological conditions. We demonstrate that physiological levels of GM(1), organized in nanodomains do not seed oligomerization of A beta(40) monomers. We show that sphingomyelin triggers oligomerization of A beta(40) and that GM(1) is counteractive thus preventing oligomerization. We propose a molecular explanation that is supported by all-atom molecular dynamics simulations. The preventive role of GM(1) in the oligomerization of A beta(40) suggests that decreasing levels of GM(1) in the brain, for example, due to aging, could reduce protection against A beta oligomerization and contribute to the onset of Alzheimer's disease.
Links
ED1.1.00/02.0068, research and development projectName: CEITEC - central european institute of technology
ED3.2.00/08.0144, research and development projectName: CERIT Scientific Cloud
GA14-12598S, research and development projectName: Samouspořádané systémy amfifilních peptiů (Acronym: SAAP)
Investor: Czech Science Foundation
LM2010005, research and development projectName: Velká infrastruktura CESNET (Acronym: VI CESNET)
Investor: Ministry of Education, Youth and Sports of the CR
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