Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)

Benedikt Frieg, Mookyoung Han, Karin Giller, Christian Dienemann, Dietmar Riedel, Stefan Becker (), Loren B. Andreas (), Christian Griesinger () and Gunnar F. Schröder ()
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Benedikt Frieg: Forschungszentrum Jülich
Mookyoung Han: Max Planck Institute for Multidisciplinary Sciences
Karin Giller: Max Planck Institute for Multidisciplinary Sciences
Christian Dienemann: Max Planck Institute for Multidisciplinary Sciences
Dietmar Riedel: Max-Planck-Institute for Multidisciplinary Sciences
Stefan Becker: Max Planck Institute for Multidisciplinary Sciences
Loren B. Andreas: Max Planck Institute for Multidisciplinary Sciences
Christian Griesinger: Max Planck Institute for Multidisciplinary Sciences
Gunnar F. Schröder: Forschungszentrum Jülich

Nature Communications, 2024, vol. 15, issue 1, 1-11

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.

Date: 2024
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DOI: 10.1038/s41467-023-43822-x

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