Structural analyses of fibrinogen amyloid fibrils

Louise C. Serpell, Merrill Benson, Juris J. Liepnieks, Paul E. Fraser

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Hereditary fibrinogen amyloidosis is characterized by deposition of amyloid fibrils in renal glomeruli. The subunit protein of the amyloid fibrils is a proteolytic fragment of the fibrinogen Aα-chain. To investigate the structure of fibrinogen amyloid, fibrils were extracted from the tissues of a patient and studied by X-ray fiber diffraction and electron microscopy. We have carried out a full structural characterization of amyloid fibrils taken from disease tissue. These studies revealed that ex vivo fibrinogen amyloid fibrils have a cross-β structure similar to other chemical types of amyloid fibrils.

Original languageEnglish (US)
Pages (from-to)199-203
Number of pages5
JournalAmyloid
Volume14
Issue number3
DOIs
StatePublished - Aug 21 2007

Keywords

  • Amyloid
  • Electron microscopy
  • Fiber diffraction
  • Fibrinogen
  • Protein structure

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Medicine(all)

Fingerprint Dive into the research topics of 'Structural analyses of fibrinogen amyloid fibrils'. Together they form a unique fingerprint.

  • Cite this

    Serpell, L. C., Benson, M., Liepnieks, J. J., & Fraser, P. E. (2007). Structural analyses of fibrinogen amyloid fibrils. Amyloid, 14(3), 199-203. https://doi.org/10.1080/13506120701461111