Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue

Marius Kollmer, William Close, Leonie Funk, Jay Rasmussen, Aref Bsoul, Angelika Schierhorn, Matthias Schmidt, Christina J. Sigurdson, Mathias Jucker and Marcus Fändrich ()
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Marius Kollmer: Ulm University
William Close: Ulm University
Leonie Funk: Ulm University
Jay Rasmussen: University of Tübingen
Aref Bsoul: Ulm University
Angelika Schierhorn: Martin-Luther-University
Matthias Schmidt: Ulm University
Christina J. Sigurdson: University of California, San Diego
Mathias Jucker: University of Tübingen
Marcus Fändrich: Ulm University

Nature Communications, 2019, vol. 10, issue 1, 1-8

Abstract: Abstract The formation of Aβ amyloid fibrils is a neuropathological hallmark of Alzheimer’s disease and cerebral amyloid angiopathy. However, the structure of Aβ amyloid fibrils from brain tissue is poorly understood. Here we report the purification of Aβ amyloid fibrils from meningeal Alzheimer’s brain tissue and their structural analysis with cryo-electron microscopy. We show that these fibrils are polymorphic but consist of similarly structured protofilaments. Brain derived Aβ amyloid fibrils are right-hand twisted and their peptide fold differs sharply from previously analyzed Aβ fibrils that were formed in vitro. These data underscore the importance to use patient-derived amyloid fibrils when investigating the structural basis of the disease.

Date: 2019
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12683-8

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DOI: 10.1038/s41467-019-12683-8

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