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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Intermediate filaments...

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Related Experiment Video

Updated: May 9, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
09:44

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

Søren Bang Nielsen1, Francesca Macchi, Samuele Raccosta

  • 1Center for Insoluble Protein Structures (inSPIN), and Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.

Plos One
|July 18, 2013
PubMed
Summary

The aggregation of alpha-synuclein (aSN) in Parkinson's Disease (PD) differs between wild-type and A30P mutant forms. Structural rearrangements continue after initial fibril formation, influencing final network density.

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Parkinson's Disease (PD) is a neurodegenerative disorder linked to alpha-synuclein (aSN) aggregation.
  • The A30P mutant of aSN is associated with early-onset familial PD and exhibits distinct aggregation properties compared to wild-type (wt) aSN.

Purpose of the Study:

  • To compare the aggregation pathways and resulting fibril network structures of wt aSN and the A30P mutant.
  • To investigate structural rearrangements occurring beyond the plateau phase of Thioflavin T (ThT) fluorescence.

Main Methods:

  • Multidisciplinary approach combining small angle X-ray scattering (SAXS), X-ray fiber diffraction, and linear dichroism.
  • Monitoring of fibril formation using Thioflavin T (ThT) fluorescence.

Main Results:

  • Both wt and A30P aSN form fibrils with a stable microscopic structure.
  • A30P aSN demonstrates a higher propensity to form dense, bundled fibril networks.
  • Wt aSN forms less dense networks, involving a rearrangement phase after the ThT fluorescence plateau.

Conclusions:

  • Structural rearrangements in aSN fibrillation can extend beyond the ThT fluorescence plateau.
  • The specific form of aSN (wt vs. A30P) significantly dictates the density and morphology of the final fibril networks.
  • Understanding these differences is crucial for comprehending PD pathogenesis.