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Structure and morphology of the Alzheimer's amyloid fibril

journal contribution
posted on 2023-06-07, 22:48 authored by Thusnelda Stromer, Louise SerpellLouise Serpell
Amyloid fibrils are deposited in a number of diseases, including Alzheimer's disease, Type 2 diabetes, and the transmissible spongiform encephalopathies (TSE). These insoluble deposits are formed from normally soluble proteins that assemble to form fibrous aggregates that accumulate in the tissues. Electron microscopy has been used as a tool to examine the structure and morphology of these aggregates from ex vivo materials, but predominantly from synthetic amyloid fibrils assembled from proteins or peptides in vitro. Electron microscopy has shown that the fibrils are straight, unbranching, and are of a similar diameter (60¿100 Å) irrespective of the precursor protein. Image processing has enhanced electron micrographs to show that amyloid fibrils appear to be composed of protofilaments wound around one another. In combination with other techniques, including X-ray fiber diffraction and solid state NMR, electron microscopy has revealed that the internal structure of the amyloid fibril is a ladder of ß-sheet structure arranged in a cross-ß conformation. Microsc. Res. Tech. 67:210¿217, 2005. © 2005 Wiley-Liss, Inc.

History

Publication status

  • Published

Journal

Microscopy Research and Technique

ISSN

1059-910X

Issue

3-4

Volume

67

Page range

210-217

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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