+検索条件
-Structure paper
タイトル | Cryo-EM structures of lipidic fibrils of amyloid-β (1-40). |
---|---|
ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 1297, Year 2024 |
掲載日 | 2024年2月13日 |
著者 | Benedikt Frieg / Mookyoung Han / Karin Giller / Christian Dienemann / Dietmar Riedel / Stefan Becker / Loren B Andreas / Christian Griesinger / Gunnar F Schröder / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:38351005 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.88 - 3.86 Å |
構造データ | EMDB-17218, PDB-8ovk: EMDB-17223, PDB-8ovm: EMDB-17234, PDB-8owd: EMDB-17235, PDB-8owe: EMDB-17238, PDB-8owj: EMDB-17239, PDB-8owk: |
由来 |
|
キーワード | PROTEIN FIBRIL / amyloid-beta (アミロイドβ) / fibril (フィブリル) / lipids (脂質) |