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001025606 1001_ $$0P:(DE-Juel1)172887$$aFrieg, Benedikt$$b0
001025606 245__ $$aCryo-EM structures of lipidic fibrils of amyloid-β (1-40)
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001025606 520__ $$aAlzheimer’s disease (AD) is a progressive and incurable neurodegenerative disease characterized by the extracellular deposition of amyloid plaques. Investigation into the composition of these plaques revealed a high amount of amyloid-β (Aβ) fibrils and a high concentration of lipids, suggesting that fibrillipid interactions may also be relevant for the pathogenesis of AD. Therefore, we grew Aβ40 fibrils in the presence of lipid vesicles and determined their structure by cryo-electron microscopy (cryo-EM) to high resolution. The fold of the major polymorph is similar to the structure of brain-seeded fibrils reported previously. The majority of the lipids are bound to the fibrils, as we show by cryo-EM and NMR spectroscopy. This apparent lipid extraction from vesicles observed here in vitro provides structural insights into potentially disease-relevant fibril-lipid interactions.
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001025606 7001_ $$00009-0004-8007-5711$$aHan, Mookyoung$$b1
001025606 7001_ $$0P:(DE-HGF)0$$aGiller, Karin$$b2
001025606 7001_ $$00000-0002-2172-5110$$aDienemann, Christian$$b3
001025606 7001_ $$0P:(DE-HGF)0$$aRiedel, Dietmar$$b4
001025606 7001_ $$00000-0003-2041-5740$$aBecker, Stefan$$b5$$eCorresponding author
001025606 7001_ $$00000-0003-3216-9065$$aAndreas, Loren B.$$b6$$eCorresponding author
001025606 7001_ $$0P:(DE-HGF)0$$aGriesinger, Christian$$b7$$eCorresponding author
001025606 7001_ $$0P:(DE-Juel1)132018$$aSchröder, Gunnar F.$$b8$$eCorresponding author
001025606 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-023-43822-x$$gVol. 15, no. 1, p. 1297$$n1$$p1297$$tNature Communications$$v15$$x2041-1723$$y2024
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