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| Hauptseite > Publikationsdatenbank > Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane > print |
| Hauptseite > Publikationsdatenbank > Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane > print |
| 001 | 902423 | ||
| 005 | 20230111074246.0 | ||
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| 245 | _ | _ | |a Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane |
| 260 | _ | _ | |a Washington, DC |c 2021 |b National Acad. of Sciences |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-mediated neuronal toxicity of amyloid-β peptides in Alzheimer’s disease. To gain a detailed understanding of the mutual interference of amyloid-β oligomers and the neuronal membrane, we carried out microseconds of all-atom molecular dynamics (MD) simulations on the dimerization of amyloid-β (Aβ)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 β-sheet transition that seems on pathway to amyloid aggregation, while the interactions with the neuronal membrane decrease the order of the Aβ42 dimer by attenuating its propensity to form a β-sheet structure. The main lipid interaction partners of Aβ42 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 Aβ-mediated toxicity. |
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| 700 | 1 | _ | |a Owen, Michael C. |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Sayyed-Ahmad, Abdallah |0 0000-0003-2415-8403 |b 3 |
| 700 | 1 | _ | |a Strodel, Birgit |0 P:(DE-Juel1)132024 |b 4 |e Corresponding author |
| 773 | _ | _ | |a 10.1073/pnas.2106210118 |g Vol. 118, no. 39, p. e2106210118 - |0 PERI:(DE-600)1461794-8 |n 39 |p e2106210118 - |t Proceedings of the National Academy of Sciences of the United States of America |v 118 |y 2021 |x 0027-8424 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/902423/files/Amyloid-%CE%B2%20peptide%20dimers%20undergo%20a%20random%20coil%20to%20%CE%B2-sheet%20transition%20in%20the%20aqueous%20phase%20but%20not%20at%20the%20neuronal%20membrane.pdf |y OpenAccess |
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