Structural properties of pore-forming oligomers of α-synuclein

Hai Young Kim, Min Kyu Cho, Ashutosh Kumar, Elke Maier, Carsten Siebenhaar, Stefan Becker, Claudio O. Fernandez, Hilal A. Lashuel, Roland Benz, Adam Lange, Markus Zweckstetter

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129 Citations (Scopus)


Soluble oligomers are potent toxins in many neurodegenerative diseases, but little is known about the structure of soluble oligomers and their structure-toxicity relationship. Here we prepared on-pathway oligomers of the 140-residue protein α-synuclein, a key player in Parkinson's disease, at concentrations an order of magnitude higher than previously possible. The oligomers form ion channels with well-defined conductance states in a variety of membranes, and their β-structure differs from that of amyloid fibrils of α-synuclein.

Original languageEnglish
Pages (from-to)17482-17489
Number of pages8
JournalJournal of the American Chemical Society
Issue number47
Publication statusPublished - 2 Dec 2009


ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Kim, H. Y., Cho, M. K., Kumar, A., Maier, E., Siebenhaar, C., Becker, S., Fernandez, C. O., Lashuel, H. A., Benz, R., Lange, A., & Zweckstetter, M. (2009). Structural properties of pore-forming oligomers of α-synuclein. Journal of the American Chemical Society, 131(47), 17482-17489.