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CPEB3 selectively inhibits α-synuclein aggregation without modulating TDP-43 pathology.

Ann Teres Babu1, Mufeeda Farhana A1, Harsha Varthini Periasamy1

  • 1School of Chemistry, Indian Institute of Science Education and Research Thiruvananthapuram (IISER TVM), Thiruvananthapuram, India.

FEBS Letters
|February 24, 2026
PubMed
Summary

The CPEB3 prion-like domain 1 (PRD1) selectively inhibits alpha-synuclein (α-Syn) amyloid aggregation, a key factor in Parkinson's disease. It does not affect TAR DNA-binding protein 43 (TDP-43) aggregation.

Keywords:
NMR spectroscopyParkinson's diseaseTDP‐43aggregation inhibitorphase separationprotein–protein interactionα‐synuclein

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Misfolded protein aggregation, including alpha-synuclein (α-Syn) and TAR DNA-binding protein 43 (TDP-43), is central to neurodegenerative diseases like Parkinson's and frontotemporal dementia.
  • Heterotypic protein aggregates are recognized for their high cytotoxicity.
  • Co-occurrence of α-Syn, TDP-43, and tau pathologies is frequent in neurodegenerative conditions.

Purpose of the Study:

  • To investigate whether the first prion-like domain (PRD1) of CPEB3 modulates the aggregation of α-Syn and TDP-43.
  • To determine the specific interactions of PRD1 with α-Syn and TDP-43 aggregates.

Main Methods:

  • Nuclear magnetic resonance (NMR) relaxation experiments to probe direct interactions.
  • Phase separation assays to evaluate liquid-liquid phase separation (LLPS)-mediated aggregation.
  • Analysis of interactions with the amyloid core of α-Syn and the C-terminal domain of TDP-43 (TDP-43CTD).

Main Results:

  • PRD1 directly interacts with the amyloid core of α-Syn, leading to suppressed aggregation.
  • Phase separation assays demonstrated that PRD1 delays α-Syn aggregation mediated by LLPS.
  • No direct interaction was observed between PRD1 and TDP-43CTD.

Conclusions:

  • CPEB3 PRD1 selectively inhibits α-Syn aggregation.
  • PRD1's interaction with α-Syn amyloid core and its effect on LLPS suggest a specific mechanism for neuroprotection.
  • These findings highlight PRD1 as a potential therapeutic target for α-Syn-related neurodegenerative diseases.