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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. 
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Amyloid Fibrils03:03

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Subviral Agents01:29

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Related Experiment Video

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Real-time Quaking-induced Conversion Assay for Detection of CWD Prions in Fecal Material
09:50

Real-time Quaking-induced Conversion Assay for Detection of CWD Prions in Fecal Material

Published on: September 29, 2017

Hot spots in prion protein for pathogenic conversion.

Kazuo Kuwata1, Noriyuki Nishida, Tomoharu Matsumoto

  • 1Center for Emerging Infectious Diseases, Department of Gene and Development, Graduate School of Medicine, Gifu University, 1-1 Yanagido, Gifu 501-1194, Japan. kuwata@gifu-u.ac.jp

Proceedings of the National Academy of Sciences of the United States of America
|July 10, 2007
PubMed
Summary

Researchers identified a chemical chaperone, GN8, that stabilizes prion protein (PrP(C)) and inhibits the pathogenic conversion to PrP(Sc), prolonging survival in transmissible spongiform encephalopathies (TSEs) models.

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

Published on: January 8, 2015

Area of Science:

  • Neuroscience
  • Biochemistry
  • Drug Discovery

Background:

  • Transmissible spongiform encephalopathies (TSEs) are linked to prion proteins.
  • The exact mechanism of prion protein (PrP(C)) conversion to the pathogenic scrapie form (PrP(Sc)) remains unclear.

Purpose of the Study:

  • To discover a chemical chaperone that stabilizes the cellular prion protein (PrP(C)) conformation.
  • To identify key "hot spots" that halt the pathogenic conversion process.

Main Methods:

  • In silico screening of compounds targeting PrP(C) conformational pockets.
  • Testing of 44 selected compounds in a TSE-infected cell culture model.
  • Administration of the identified compound in TSE-infected mice and analysis using Heteronuclear NMR and computer simulation.

Main Results:

  • One compound, GN8, significantly reduced PrP(Sc) levels in cell cultures.
  • GN8 administration prolonged survival in mice infected with TSEs.
  • NMR and simulations identified specific binding sites (A-S2 loop and helix B to B-C loop regions) that impede pathogenic conversion.

Conclusions:

  • GN8 acts as a chemical chaperone, stabilizing PrP(C) and inhibiting PrP(Sc) formation.
  • Targeting identified "hot spots" is a viable strategy for developing novel anti-prion drugs.
  • A dynamics-based drug discovery approach focusing on PrP(C) hot spots shows promise for combating prion diseases.