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Common core structure of amyloid fibrils by synchrotron X-ray diffraction
journal contribution
posted on 2023-06-07, 19:40 authored by Margaret Sunde, Louise SerpellLouise Serpell, Mark Bartlam, Paul E Fraser, Mark B Pepys, Colin C F BlakeTissue deposition of normally soluble proteins as insoluble amyloid fibrils is associated with serious diseases including the systemic amyloidoses, maturity onset diabetes, Alzheimer's disease and transmissible spongiform encephalopathy. Although the precursor proteins in different diseases do not share sequence homology or related native structure, the morphology and properties of all amyloid fibrils are remarkably similar. Using intense synchrotron sources we observed that six different ex vitro amyloid fibrils and two synthetic fibril preparations all gave similar high-resolution X-ray fibre diffraction patterns, consistent with a helical array of ß-sheets parallel to the fibre long axis, with the strands perpendicular to this axis. This confirms that amyloid fibrils comprise a structural superfamily and share a common protofilament substructure, irrespective of the nature of their precursor proteins.
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Publication status
- Published
Journal
Journal of Molecular BiologyISSN
00222836External DOI
Issue
3Volume
273Page range
729-739Department affiliated with
- Biochemistry Publications
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- No
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- Yes
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2012-02-06Usage metrics
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