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August 8, 2024FEBS JournalOpen Access

Liquid–liquid phase separation of alpha‐synuclein increases the structural variability of fibrils formed during amyloid aggregation

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Authors

MŽMantas ŽiaunysVilnius UniversityDŠDarius ŠulskisVilnius UniversityDVDominykas VeiverisVilnius University

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Overview

Comparative analysis shows increased structural diversity and toxicity in alpha-synuclein fibrils, suggesting condensate formation drives pathogenic variant emergence.

Key Points

  • Phase separation of alpha-synuclein drives diverse amyloid aggregation pathways, yielding distinct secondary structures alongside varied fibril morphologies.
  • Comparative analysis of alpha-synuclein under liquid-liquid phase separation conditions shows formed assemblies exhibit markedly higher cellular toxicity.
  • Biomolecular condensate formation may represent a critical pathological step in neurodegenerative disorders—in vitro cell model; further validation needed.

Cite This Study

Žiaunys et al. (2024) studied this question.

synapsesocial.com/papers/68e5cfeeb6db643587565eadhttps://doi.org/10.1111/febs.17244
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Also Consider

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