(GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced
bySphingomyelin

J 2016

(GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin

AMARO, Mariana; Radek ŠACHL; Gokcan AYDOGAN; Ilya I. MIKHALYOV; Robert VÁCHA et al.

Základní údaje

Originální název

(GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin

Autoři

AMARO, Mariana; Radek ŠACHL; Gokcan AYDOGAN; Ilya I. MIKHALYOV; Robert VÁCHA a Martin HOF

Vydání

Angewandte Chemie International Edition, WEINHEIM, Wiley-V C H VERLAG GMBH, 2016, 1433-7851

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 11.994

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/16:00088531

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

Alzheimer's disease; amyloid beta-peptides; diffusion coefficients; fluorescence spectroscopy; neuroprotectives

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 1. 3. 2017 13:59, Mgr. Eva Špillingová

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

ED3.2.00/08.0144, projekt VaV

Název: CERIT Scientific Cloud

GA14-12598S, projekt VaV

Název: Samouspořádané systémy amfifilních peptiů (Akronym: SAAP)

Investor: Grantová agentura ČR, Self-assembly of amphiphilic peptides with helical character

LM2010005, projekt VaV

Název: Velká infrastruktura CESNET (Akronym: VI CESNET)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Velká infrastruktura CESNET

Citovat

AMARO, Mariana; Radek ŠACHL; Gokcan AYDOGAN; Ilya I. MIKHALYOV; Robert VÁCHA a Martin HOF. (GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin. Angewandte Chemie International Edition. WEINHEIM: Wiley-V C H VERLAG GMBH, 2016, roč. 55, č. 32, s. 9411-9415. ISSN 1433-7851. Dostupné z: https://doi.org/10.1002/anie.201603178.

@article{1367185,
   author = {Amaro, Mariana and Šachl, Radek and Aydogan, Gokcan and Mikhalyov, Ilya I. and Vácha, Robert and Hof, Martin},
   article_location = {WEINHEIM},
   article_number = {32},
   doi = {https://doi.org/10.1002/anie.201603178},
   keywords = {Alzheimer's disease; amyloid beta-peptides; diffusion coefficients; fluorescence spectroscopy; neuroprotectives},
   language = {eng},
   issn = {1433-7851},
   journal = {Angewandte Chemie International Edition},
   title = {(GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin},
   url = {http://onlinelibrary.wiley.com/doi/10.1002/anie.201603178/abstract},
   volume = {55},
   year = {2016}
}

TY  - JOUR
ID  - 1367185
AU  - Amaro, Mariana - Šachl, Radek - Aydogan, Gokcan - Mikhalyov, Ilya I. - Vácha, Robert - Hof, Martin
PY  - 2016
TI  - (GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin
JF  - Angewandte Chemie International Edition
VL  - 55
IS  - 32
SP  - 9411-9415
EP  - 9411-9415
PB  - Wiley-V C H VERLAG GMBH
SN  - 14337851
KW  - Alzheimer's disease
KW  - amyloid beta-peptides
KW  - diffusion coefficients
KW  - fluorescence spectroscopy
KW  - neuroprotectives
UR  - http://onlinelibrary.wiley.com/doi/10.1002/anie.201603178/abstract
L2  - http://onlinelibrary.wiley.com/doi/10.1002/anie.201603178/abstract
N2  - 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.
ER  -

AMARO, Mariana; Radek ŠACHL; Gokcan AYDOGAN; Ilya I. MIKHALYOV; Robert VÁCHA a Martin HOF. (GM1) Ganglioside Inhibits beta-Amyloid Oligomerization Induced bySphingomyelin. \textit{Angewandte Chemie International Edition}. WEINHEIM: Wiley-V C H VERLAG GMBH, 2016, roč.~55, č.~32, s.~9411-9415. ISSN~1433-7851. Dostupné z: https://doi.org/10.1002/anie.201603178.

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