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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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,...
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A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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Synthetic Sulfated Polymers Control Amyloid Aggregation of Ovine Prion Protein and Decrease Its Toxicity.

Pavel Semenyuk1, Diana Evstafyeva1, Vladimir Izumrudov2

  • 1Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia.

Polymers
|April 12, 2022
PubMed
Summary
This summary is machine-generated.

Sulfonated polymers show potential in treating prion protein aggregation, a cause of amyloidosis. Certain polymers like poly(styrene sulfonate) inhibit amyloid formation and reduce cytotoxicity, offering new therapeutic avenues.

Keywords:
amyloidamyloidosisartificial chaperonepolyanionpolystyrene sulfonateprion protein

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Polymer Science

Background:

  • Amyloid aggregation, particularly prion protein (PrP) aggregation, is central to amyloidosis, a group of diseases with limited treatment options.
  • Prionopathies, affecting humans and animals, involve the accumulation of misfolded prion protein.

Purpose of the Study:

  • To investigate the impact of sulfated/sulfonated polymers on prion protein amyloidogenic conversion and aggregation.
  • To evaluate the potential of these polymers as therapeutic agents against prion diseases and amyloidosis.

Main Methods:

  • In vitro experiments using ovine prion protein and various sulfated/sulfonated polymers (sodium dextran sulfate, polystyrene sulfonate, polyanethole sulfonate, polyvinyl sulfate).
  • Molecular dynamics simulations to understand polymer-protein interactions.
  • Seeding experiments and cytotoxicity assays to assess amyloidogenic capacity and cellular toxicity.

Main Results:

  • All tested polymers induced amyloid conversion of the prion protein, likely by destabilizing its native structure.
  • Short polymers promoted aggregation, while high-molecular poly(styrene sulfonate) inhibited fibril formation.
  • Poly(styrene sulfonate) significantly reduced the amyloidogenic capacity of protein-polymer complexes and completely inhibited the cytotoxicity of soluble oligomers.

Conclusions:

  • Sulfonated polymers, especially poly(styrene sulfonate), demonstrate significant anti-prion and anti-amyloidosis properties.
  • These polymers represent a promising platform for developing novel therapeutics for prionopathies and other amyloid diseases.