Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)
2024 | journal article. A publication with affiliation to the University of Göttingen.
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Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)
Frieg, B.; Han, M.; Giller, K.; Dienemann, C.; Riedel, D.; Becker, S. & Andreas, L. B. et al. (2024)
Nature Communications, 15(1). DOI: https://doi.org/10.1038/s41467-023-43822-x
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Details
- Authors
- Frieg, Benedikt; Han, Mookyoung; Giller, Karin; Dienemann, Christian; Riedel, Dietmar; Becker, Stefan; Andreas, Loren B.; Griesinger, Christian; Schröder, Gunnar F.
- Abstract
- Abstract Alzheimer’s disease (AD) is a progressive and incurable neurodegenerative disease characterized by the extracellular deposition of amyloid plaques. Investigation into the composition of these plaques revealed a high amount of amyloid-β (Aβ) fibrils and a high concentration of lipids, suggesting that fibril-lipid interactions may also be relevant for the pathogenesis of AD. Therefore, we grew Aβ40 fibrils in the presence of lipid vesicles and determined their structure by cryo-electron microscopy (cryo-EM) to high resolution. The fold of the major polymorph is similar to the structure of brain-seeded fibrils reported previously. The majority of the lipids are bound to the fibrils, as we show by cryo-EM and NMR spectroscopy. This apparent lipid extraction from vesicles observed here in vitro provides structural insights into potentially disease-relevant fibril-lipid interactions.
- Issue Date
- 2024
- Journal
- Nature Communications
- Project
- EXC 2067: Multiscale Bioimaging
- Working Group
- RG Griesinger
- eISSN
- 2041-1723
- Language
- English