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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...
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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Ion-specific effects on prion nucleation and strain formation.

Jonathan Rubin1, Hasan Khosravi2, Kathryn L Bruce3

  • 1From the School of Chemical and Biomolecular Engineering,; Parker H. Petit Institute of Bioengineering and Bioscience.

The Journal of Biological Chemistry
|August 31, 2013
PubMed
Summary

Hofmeister ions influence amyloid formation. Kosmotropes promote rapid amyloid nucleation and specific strains with distinct in vivo phenotypes, unlike chaotropes.

Keywords:
AmyloidChaotropeHofmeister SeriesKosmotropeProtein AggregationProtein ConformationTranslation Release FactorsYeast

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Last Updated: May 8, 2026

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Aggregation

Background:

  • Amyloids are ordered protein aggregates linked to diseases and heritable traits.
  • Different amyloid conformations (strains) cause distinct phenotypes.
  • The role of Hofmeister ions in amyloid strain selection is not well understood.

Purpose of the Study:

  • To investigate the impact of Hofmeister ions on amyloid nucleation and strain generation.
  • To characterize the properties of amyloids formed under different ionic conditions.

Main Methods:

  • Studied amyloid nucleation and fiber elongation using the yeast Sup35NM prion domain fragment.
  • Utilized kosmotropic and chaotropic anions to probe Hofmeister ion effects.
  • Assessed amyloid strain properties including thermostability, frangibility, and in vivo phenotypes.

Main Results:

  • Kosmotropic anions accelerated amyloid nucleation and fiber elongation compared to chaotropic anions.
  • Kosmotropes favored the formation of amyloid strains with lower thermostability and higher frangibility in vitro.
  • Amyloids formed in kosmotropes exhibited stronger in vivo phenotypic effects and proliferation patterns.

Conclusions:

  • Ionic composition significantly influences amyloid nucleation kinetics and strain selection.
  • Hofmeister ions, through their hydration properties, dictate the preferential formation of specific amyloid strains.
  • This study reveals a direct link between ion biochemistry and the resulting amyloid strain characteristics.