University of Sussex
Browse

File(s) not publicly available

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 Blake
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 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.

History

Publication status

  • Published

Journal

Journal of Molecular Biology

ISSN

00222836

Issue

3

Volume

273

Page range

729-739

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC