Synthetic filaments assembled from C-terminally truncated alpha-synuclein

FEBS Lett. 1998 Oct 9;436(3):309-12. doi: 10.1016/s0014-5793(98)01146-6.


Recently two point mutations in the alpha-synuclein gene have been found in familial Parkinson's disease. The characteristic fibrous neuropathological lesions of Parkinson's and other neurodegenerative diseases have been shown to stain strongly with antibodies against alpha-synuclein and extracted filaments have been labelled with anti-alpha-synuclein antibodies. In view of the close involvement of alpha-synuclein filaments with pathology, it was important to establish an in vitro assembly system. We report here that C-terminally truncated recombinant alpha-synuclein readily assembles into filaments resembling those isolated from diseased brain and suggest that truncation by proteolysis may play a role in the pathological process.

MeSH terms

  • Alanine
  • Amino Acid Substitution
  • Cloning, Molecular
  • Humans
  • Microscopy, Electron
  • Mutagenesis, Site-Directed
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / ultrastructure*
  • Open Reading Frames
  • Phosphoproteins / chemistry
  • Phosphoproteins / ultrastructure
  • Point Mutation
  • Proline
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / ultrastructure
  • Sequence Deletion
  • Synucleins
  • Threonine
  • alpha-Synuclein


  • Nerve Tissue Proteins
  • Phosphoproteins
  • Recombinant Proteins
  • SNCA protein, human
  • Synucleins
  • alpha-Synuclein
  • Threonine
  • Proline
  • Alanine