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Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue
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Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue
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Journal Article
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue
2019
Overview
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.
Alzheimer’s disease is characterised by the deposition of Aβ amyloid fibrils and tau protein neurofibrillary tangles. Here the authors use cryo-EM to structurally characterise brain derived Aβ amyloid fibrils and find that they are polymorphic and right-hand twisted, which differs from in vitro generated Aβ fibrils.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 147/135
/ 147/143
/ 631/45
/ 82/1
/ 82/29
/ 82/58
/ Alzheimer Disease - metabolism
/ Alzheimer Disease - pathology
/ Amyloid beta-Peptides - metabolism
/ Brain
/ Cryoelectron Microscopy - methods
/ Humanities and Social Sciences
/ Humans
/ Patients
/ Peptides
/ Proteins
/ Scanning electron microscopy
/ Science
