Amyloid-beta peptide dimers undergo a random coil to beta-sheet transition in the aqueous phase but not at the neuronal membrane
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00124309" target="_blank" >RIV/00216224:14740/21:00124309 - isvavai.cz</a>
Result on the web
<a href="https://www.pnas.org/content/118/39/e2106210118" target="_blank" >https://www.pnas.org/content/118/39/e2106210118</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1073/pnas.2106210118" target="_blank" >10.1073/pnas.2106210118</a>
Alternative languages
Result language
angličtina
Original language name
Amyloid-beta peptide dimers undergo a random coil to beta-sheet transition in the aqueous phase but not at the neuronal membrane
Original language description
Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-mediated neuronal toxicity of amyloid-beta peptides in Alzheimer's disease. To gain a detailed understanding of the mutual interference of amyloid-beta oligomers and the neuronal membrane, we carried out microseconds of all-atom molecular dynamics (MD) simulations on the dimerization of amyloid-beta (A beta)42 in the aqueous phase and in the presence of a lipid bilayer mimicking the in vivo composition of neuronal membranes. The dimerization in solution is characterized by a random coil to beta-sheet transition that seems on pathway to amyloid aggregation, while the interactions with the neuronal membrane decrease the order of the A beta 42 dimer by attenuating its propensity to form a beta-sheet structure. The main lipid interaction partners of A beta 42 are the surface-exposed sugar groups of the gangliosides GM1. As the neurotoxic activity of amyloid oligomers increases with oligomer order, these results suggest that GM1 is neuroprotective against A beta-mediated toxicity.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424
e-ISSN
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Volume of the periodical
118
Issue of the periodical within the volume
39
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
„e2106210118“
UT code for WoS article
000708052600007
EID of the result in the Scopus database
2-s2.0-85115315726