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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
Full text not available from this repository.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 |