Abstract:
:Tissue 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 vivo amyloid fibrils and two synthetic fibril preparations all gave similar high-resolution X-ray fibre diffraction patterns, consistent with a helical array of beta-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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Sunde M,Serpell LC,Bartlam M,Fraser PE,Pepys MB,Blake CCdoi
10.1006/jmbi.1997.1348subject
Has Abstractpub_date
1997-10-31 00:00:00pages
729-39issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(97)91348-6journal_volume
273pub_type
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