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Using leucine zipper to facilitate alpha-synuclein assembly.

Peizhou Jiang1, Li-wen Ko, Karen R Jansen

  • 1Department of Neuroscience, Mayo Clinic College of Medicine, 4500 San Pablo Rd., Jacksonville, FL 32224, USA.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|May 22, 2008
PubMed
Summary

Filamentous alpha-synuclein (alpha-S) assembly in Parkinson's disease can occur in parallel or antiparallel modes, with antiparallel assembly being more prevalent. This study shows artificial zippers accelerate alpha-S assembly and aid in developing cellular models for drug screening.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • Filamentous alpha-synuclein (alpha-S) accumulation is a hallmark of Parkinson's disease.
  • The precise mechanism and structural requirements of alpha-S self-assembly remain incompletely understood.
  • Controversy exists regarding the parallel versus antiparallel orientation of alpha-S filaments and the necessity of hydrophobic region alignment.

Purpose of the Study:

  • To investigate the influence of artificial leucine zippers (Zips) on alpha-S filament assembly.
  • To determine whether alpha-S can assemble in both parallel and antiparallel modes.
  • To assess the necessity of precise central hydrophobic region alignment during alpha-S self-assembly.
  • To establish a cellular model for screening alpha-S assembly inhibitors.

Main Methods:

  • In vitro assembly of alpha-S with and without Zip-fused derivatives (parallel, antiparallel, and with a spacer).
  • Thioflavin T (ThT) fluorescence assays to quantify filament formation.
  • Cellular expression of Zip-fused alpha-S and alpha-S alone.
  • Immunofluorescence and thioflavin S staining to detect alpha-S inclusions in cells.

Main Results:

  • Artificial Zips significantly accelerated alpha-S filament assembly in both parallel and antiparallel configurations.
  • A precise alignment of the central hydrophobic region of alpha-S was not essential for filament formation.
  • Antiparallel alpha-S pairs exhibited higher ThT fluorescence signals compared to parallel arrangements.
  • Cells overexpressing Zip-fused alpha-S formed alpha-S immunopositive and thioflavin S-positive inclusions within 7 days, unlike cells expressing alpha-S alone.

Conclusions:

  • Alpha-synuclein (alpha-S) self-assembly occurs in both parallel and antiparallel modes, with a greater propensity for antiparallel assembly.
  • The precise alignment of the central hydrophobic region is not critical for alpha-S filament formation.
  • Zip-fused alpha-S expressing cells provide a robust model for screening inhibitors of alpha-S aggregation, relevant to Parkinson's disease research.