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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

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Alternative Structures of α-Synuclein.

Dawid Dułak1, Małgorzata Gadzała2, Mateusz Banach3

  • 1Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, Łojasiewicza 11, 30-348 Kraków, Poland.

Molecules (Basel, Switzerland)
|February 6, 2020
PubMed
Summary
This summary is machine-generated.

Alpha-synuclein (ASyn) misfolding is linked to Parkinson's disease. Our study shows that ASyn fragments not involved in amyloid fibrils can form globular structures, influencing disease mechanisms.

Keywords:
A-synucleinamyloidfibrilhydrophobicitymisfoldingprotein folding

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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

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Area of Science:

  • Structural biology
  • Neuroscience
  • Biophysics

Background:

  • Alpha-synuclein (ASyn) misfolding and aggregation are implicated in Parkinson's disease pathogenesis.
  • ASyn's structure varies between micelle-bound and amyloid forms, with only the central fragment (30-100) forming fibrils, while N- and C-terminal regions (1-30, 100-140) remain disordered.
  • Understanding ASyn's conformational flexibility is crucial for elucidating its role in disease.

Purpose of the Study:

  • To investigate whether the ASyn chain and its individual fragments can adopt globular conformations.
  • To explore the structural basis of ASyn's amyloid transformation and its relationship with Parkinson's disease.
  • To analyze the influence of mutations on ASyn's amyloidogenic potential.

Main Methods:

  • Computational protein structure prediction using Robetta and I-Tasser.
  • Application of the Fuzzy Oil Drop (FOD) model to simulate solvent effects on protein structure.
  • Comparative analysis of predicted structures for ASyn fragments and the full chain.

Main Results:

  • ASyn fragments 1-30 and 100-140, which are disordered in amyloid fibrils, can adopt globular conformations.
  • The central fragment (30-100) does not form a centralized hydrophobic core, favoring ribbonlike micelle formation over spherical structures.
  • The study provides insights into how ASyn's conformational preferences and environmental factors drive its aggregation pathway.

Conclusions:

  • Disordered ASyn fragments possess the intrinsic ability to form globular structures.
  • The ribbonlike micelle structure of ASyn represents an adaptation to minimize hydrophobic exposure to the aqueous solvent.
  • These findings contribute to understanding the structural dynamics of ASyn in relation to Parkinson's disease.