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TitleElucidating the Unique J-Shaped Protomer Structure of Amyloid-β(1-40) Fibril with Cryo-Electron Microscopy.
Journal, issue, pagesInt J Mol Sci, Vol. 26, Issue 3, Year 2025
Publish dateJan 29, 2025
AuthorsRaymond N Burton-Smith / Maho Yagi-Utsumi / Saeko Yanaka / Chihong Song / Kazuyoshi Murata / Koichi Kato /
PubMed AbstractAlthough the structural diversity of amyloid-β (Aβ) fibrils plays a critical role in the pathology of Alzheimer's disease (AD), the mechanisms underlying this diversity remain poorly understood. In ...Although the structural diversity of amyloid-β (Aβ) fibrils plays a critical role in the pathology of Alzheimer's disease (AD), the mechanisms underlying this diversity remain poorly understood. In this study, we report the discovery of a novel J-shaped protomer structure of Aβ40 fibrils, resolved at 3.3 Å resolution using cryo-electron microscopy. Under controlled conditions (20 mM sodium phosphate buffer, pH 8.0) designed to emphasize intra-protomer interactions and slow fibril elongation, the J-shaped structure revealed distinct salt bridges (e.g., D1-K28, R5-E22) that stabilize the fibril core. These findings expand our understanding of the free energy landscape of fibril formation, shedding light on how specific environmental factors, such as pH and ionic strength, may influence fibril polymorphism. Importantly, the unique features of the J-shaped protomer provide insights into the structural basis of amyloid plaque diversity in AD and suggest potential therapeutic strategies targeting intra-protomer interactions. This study underscores the importance of fibril polymorphism in AD pathology and offers a foundation for future research into fibril-targeted therapies.
External linksInt J Mol Sci / PubMed:39940945 / PubMed Central
MethodsEM (helical sym.)
Resolution3.3 Å
Structure data

60603

9iio

EMDB-60603, PDB-9iio:
J-shaped conformer of amyloid beta (1-40)
Method: EM (helical sym.) / Resolution: 3.3 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Amyloid

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