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Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy
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Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy
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Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy
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Journal Article
Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy
2008
Overview
Alzheimer's disease is a neurodegenerative disorder that is characterized by the cerebral deposition of amyloid fibrils formed by Aβ peptide. Despite their prevalence in Alzheimer's and other neurodegenerative diseases, important details of the structure of amyloid fibrils remain unknown. Here, we present a three-dimensional structure of a mature amyloid fibril formed by Aβ(1-40) peptide, determined by electron cryomicroscopy at [almost equal to]8-Å resolution. The fibril consists of two protofilaments, each containing [almost equal to]5-nm-long regions of β-sheet structure. A local twofold symmetry within each region suggests that pairs of β-sheets are formed from equivalent parts of two Aβ(1-40) peptides contained in each protofilament. The pairing occurs via tightly packed interfaces, reminiscent of recently reported steric zipper structures. However, unlike these previous structures, the β-sheet pairing is observed within an amyloid fibril and includes significantly longer amino acid sequences.
