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Updated: Jul 13, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
Structural analyses of fibrinogen amyloid fibrils
Louise C Serpell1, Merrill Benson, Juris J Liepnieks
1Biochemistry, University of Sussex, John Maynard-Smith Building, Falmer, Brighton, UK. L.C.Serpell@sussex.ac.uk
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 Aalpha-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-beta structure similar to other chemical types of amyloid fibrils.
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