Structure and textures of fibrous crystals of the Abeta (11-25) peptide fragment from Alzheimer's Abeta Amyloid protein.

Sikorski, Pawel, Atkins, Edward D T and Serpell, Louise C (2003) Structure and textures of fibrous crystals of the Abeta (11-25) peptide fragment from Alzheimer's Abeta Amyloid protein. Structure, 11 (1). pp. 1-2. ISSN 0969-2126

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Abstract

Amyloid fibril deposition is central to the pathology of Alzheimer's disease. X-ray diffraction from amyloid fibrils formed from full-length Aß(1¿40) and from a shorter fragment, Aß(11¿25), have revealed cross-ß diffraction fingerprints. Magnetic alignment of Aß(11¿25) amyloid fibrils gave a distinctive X-ray diffraction texture, allowing interpretation of the diffraction data and a model of the arrangement of the peptides within the amyloid fiber specimen to be constructed. An intriguing feature of the structure of fibrillar Aß(11¿25) is that the ß sheets, of width 5.2 nm, stack by slipping relative to each other by the length of two amino acid units (0.70 nm) to form ß ribbons 4.42 nm in thickness. Aß(1¿40) amyloid fibrils likely consist of once-folded hairpins, consistent with the size of the fibers obtained using electron microscopy and X-ray diffraction.

Item Type: Article
Additional Information: LS is the senior author, collected the data and wrote the paper. This paper revealed the arrangement of Alzheimer's peptide within amyloid fibrils, cited 37 times.
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Louise Serpell
Date Deposited: 06 Feb 2012 21:08
Last Modified: 26 Mar 2012 09:42
URI: http://sro.sussex.ac.uk/id/eprint/29739
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