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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • 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

  • 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