Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

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 Biol

authors

Sunde M,Serpell LC,Bartlam M,Fraser PE,Pepys MB,Blake CC

doi

10.1006/jmbi.1997.1348

subject

Has Abstract

pub_date

1997-10-31 00:00:00

pages

729-39

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(97)91348-6

journal_volume

273

pub_type

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