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Related Concept Videos

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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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Published on: July 16, 2008

Structural insights into alternate aggregated prion protein forms.

Maurizio Polano1, Alpan Bek, Federico Benetti

  • 1Laboratory of Prion Biology, Neurobiology Sector, Scuola Internazionale Superiore di Studi Avanzati-International School of Advanced Studies (SISSA-ISAS) Edificio Q1, Area Science Park, SS 14 Km 163.5, I-34149 Basovizza (TS), Italy.

Journal of Molecular Biology
|September 2, 2009
PubMed
Summary

Researchers explored how chemical conditions influence prion protein (PrP) structures. Altering guanidine hydrochloride concentrations changed PrP aggregate formation, impacting potential prion infectivity and toxicity.

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Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Published on: December 19, 2015

Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Prion diseases involve the misfolding of cellular prion protein (PrP(C)) into abnormal isoforms (PrP(Sc)).
  • Synthetic prions generated from recombinant PrP (recPrP) can cause novel prion diseases.
  • Amyloid seeding assays using recPrP can detect and amplify prion strains.

Purpose of the Study:

  • To analyze the morphology of PrP aggregate structures under varying chemical constraints.
  • To investigate the influence of guanidine hydrochloride concentration on PrP aggregation kinetics and structure.

Main Methods:

  • Utilized an amyloid seeding assay with recombinant mouse PrP (residues 89-230).
  • Employed thioflavin T (ThT) fluorescence assay to monitor aggregation kinetics.
  • Conducted atomic force microscopy (AFM) for morphological and structural analysis of aggregates.

Main Results:

  • Guanidine hydrochloride concentration affected kinetic traces in the ThT assay.
  • Low guanidine hydrochloride concentrations favored oligomeric PrP structures.
  • Higher guanidine hydrochloride concentrations promoted the formation of more amyloid-like PrP structures.

Conclusions:

  • Chemical constraints, specifically guanidine hydrochloride concentration, modulate the structural assembly of PrP.
  • PrP aggregate morphology varies from oligomeric to amyloid structures based on denaturant concentration.
  • These findings suggest complex pathways govern prion infectivity and toxicity.