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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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Temperature profoundly affects ataxin-3 fibrillogenesis.

Alessandra Apicella1, Antonino Natalello, Anna Maria Frana

  • 1Department of Energy and NEMAS, Center for NanoEngineered Materials and Surfaces, Politecnico di Milano, via Ponzio 34/3 I-20133 Milano, Italy.

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Temperature significantly alters the aggregation of Ataxin-3 (AT3) variants. While normal AT3 aggregates similarly at different temperatures, expanded AT3 forms amorphous aggregates at higher temperatures, suggesting a distinct fibrillogenesis mechanism.

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Area of Science:

  • Biochemistry
  • Neurodegenerative Diseases
  • Protein Misfolding

Background:

  • Ataxin-3 (AT3) protein aggregation is linked to spinocerebellar ataxia type 3 (SCA3).
  • Polyglutamine (polyQ) tract length in AT3 influences its aggregation propensity.
  • Previous studies indicated AT3Q55 forms irreversible fibrils at 37°C, unlike AT3Q24.

Purpose of the Study:

  • To investigate the effect of elevated temperature (up to 85°C) on the aggregation of normal (AT3Q24) and expanded (AT3Q55) Ataxin-3 variants.
  • To elucidate the temperature-dependent mechanism of Ataxin-3 fibrillogenesis.

Main Methods:

  • Fourier transform infrared spectroscopy (FTIR)
  • Atomic force microscopy (AFM)
  • Controlled temperature incubation (37°C to 85°C)

Main Results:

  • AT3Q24, when heated to 85°C, exhibited aggregation patterns similar to those observed at 37°C.
  • In contrast, AT3Q55, when heated to 85°C, formed large, amorphous aggregates, differing from the fibrillar structures seen at 37°C.
  • Temperature significantly modulates the aggregation pathway and final structure of AT3 variants.

Conclusions:

  • Temperature plays a critical role in determining the outcome of Ataxin-3 aggregation.
  • The expanded polyQ tract in AT3Q55 leads to temperature-sensitive aggregation, favoring amorphous structures at higher temperatures.
  • These findings offer insights into the differential mechanisms of Ataxin-3 fibrillogenesis under varying thermal conditions.