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α-Synuclein Aggregation Intermediates form Fibril Polymorphs with Distinct Prion-like Properties.

Surabhi Mehra1, Sahil Ahlawat2, Harish Kumar3

  • 1Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India. Electronic address: https://twitter.com/SurabhiMehra5.

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Summary

Alpha-synuclein (α-Syn) fibril polymorphs exhibit distinct structures and cellular activities. This study reveals how α-Syn aggregation intermediates lead to diverse, prion-like behaviors in synucleinopathies.

Keywords:
amyloidspolymorphssynucleinopathiesα-Synuclein

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Synucleinopathies, such as Parkinson's disease, involve alpha-synuclein (α-Syn) amyloid formation.
  • The structural diversity and prion-like strain behavior of α-Syn amyloids are increasingly recognized but poorly understood.
  • The mechanisms generating different α-Syn fibril polymorphs from the same precursor protein remain elusive.

Purpose of the Study:

  • To investigate the structure-function relationship of distinct α-Syn fibril polymorphs.
  • To elucidate how different α-Syn aggregation intermediates influence fibril structure and cellular activity.
  • To understand the implications of conformational heterogeneity in α-Syn aggregation for prion-like behavior.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (ssNMR) spectroscopy.
  • Mass spectrometry.
  • Cellular assays assessing seeding, internalization, and cell-to-cell transfer of α-Syn aggregates.

Main Results:

  • Two α-Syn polymorphs, pre-matured fibrils (PMFs) and helix-matured fibrils (HMFs), were characterized.
  • HMFs possess a compact core structure, showing low seeding potency but efficient cellular internalization and transfer.
  • PMFs, less structured, lack transcellular transfer but induce significant α-Syn pathology and aggresome formation.

Conclusions:

  • Conformational heterogeneity during α-Syn aggregation generates distinct fibril polymorphs.
  • These polymorphs exhibit differential cellular activities, including seeding, internalization, and cell-to-cell propagation.
  • The findings highlight the potential for diverse, prion-like behaviors arising from α-Syn aggregation intermediates in synucleinopathies.