(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 (203 Česká republika), Radek ŠACHL (203 Česká republika), Gokcan AYDOGAN (203 Česká republika), Ilya I. MIKHALYOV (643 Rusko), Robert VÁCHA (203 Česká republika, garant, domácí) a Martin HOF (276 Německo)

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

Kód RIV

RIV/00216224:14740/16:00088531

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1002/anie.201603178

UT WoS

000383371800055

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://dx.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 = {http://dx.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://dx.doi.org/10.1002/anie.201603178.

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