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Sequence- and seed-structure-dependent polymorphic fibrils of alpha-synuclein.

Goki Tanaka1, Tomoyuki Yamanaka1, Yoshiaki Furukawa2

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Biochimica Et Biophysica Acta. Molecular Basis of Disease
|February 22, 2019
PubMed
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Alpha-synuclein (a-syn) aggregates differ structurally between humans and mice. Specific mutations, like A53T in Parkinson's disease, influence aggregate structure and transmissibility, impacting neurodegenerative disease research.

Keywords:
Alpha-synucleinAmyloid fibrilsInterspecies differenceParkinson's diseaseProtein aggregation

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Area of Science:

  • Neurodegenerative diseases
  • Protein misfolding and aggregation
  • Structural biology

Background:

  • Synucleinopathies, including Parkinson's disease, are characterized by alpha-synuclein (a-syn) aggregation.
  • Human and mouse a-syn sequences differ at seven positions, potentially affecting aggregate structure.

Purpose of the Study:

  • To characterize structural differences between human and mouse a-syn aggregates.
  • To investigate the role of sequence variations and mutations in a-syn aggregate formation and structure.
  • To determine the transmissibility of a-syn aggregate structures.

Main Methods:

  • In vitro aggregation of human and mouse alpha-synuclein.
  • Morphological analysis of amyloid fibrils using microscopy.
  • Protease resistance assays to identify core regions.
  • Seeding experiments with mutated alpha-synuclein.

Main Results:

  • Human and mouse a-syn formed distinct amyloid fibril structures (twisted vs. straight).
  • Different protease-resistant core regions (long vs. short) were identified.
  • The A53T mutation in human a-syn induced a structural conversion to straight fibrils with short cores.
  • Seeding with A53T aggregates resulted in straight-type fibrils with short cores.

Conclusions:

  • Alpha-synuclein aggregate structure is sequence-dependent during spontaneous aggregation.
  • Aggregate structure becomes dependent on seeding conditions when templates are introduced.
  • Understanding these structural variations is crucial for modeling synucleinopathies and developing therapeutics.