Single-molecule nanopore dielectrophoretic trapping of α-synuclein with lipid membranes

Jinming Wu, Tohru Yamashita, Andrew D. Hamilton, Sam Thompson, Jinghui Luo

Research output: Contribution to journalArticlepeer-review


The lipid-α-Synuclein (α-Syn) interaction plays a crucial role in the pathogenesis of Parkinson's disease. Here, we investigate the lipid-binding and -unbinding kinetics of α-Syn in an α-hemolysin (αHL) single nanopore. Under an applied voltage, an engineered α-Syn sequence can be trapped at the nanopore due to the dielectrophoretic force. The conformational switch events of α-Syn can be observed at the pore-membrane junction through the interpretation of blockade current amplitudes and dwell time. This allows further analysis of α-Syn conformational dynamics. We study how disease-associated metal ions (Cu2+, Zn2+) modulate the dynamics of α-Syn at the interface of the membranes and pore and how α-helical peptidomimetics stabilize the helical conformation of α-Syn in a lipidic environment. These studies aid our understanding of the complexity of the interaction of α-Syn, lipid membranes, and metal ions, and in using peptidomimetics, a new strategy against α-Syn toxicity and aggregation is advanced.

Original languageEnglish (US)
Article number101243
JournalCell Reports Physical Science
Issue number2
StatePublished - Feb 15 2023


  • lipid bilayer
  • nanopore
  • neurodegeneration, Parkinson's disease, metal ions, trapping.
  • peptidomimetic
  • α-Synuclein

ASJC Scopus subject areas

  • General Chemistry
  • General Materials Science
  • General Engineering
  • General Energy
  • General Physics and Astronomy


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