Aarhus Universitets segl

The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

  • Nikolai Lorenzen, Danmark
  • Lasse Lemminger, Danmark
  • Jannik Nedergaard Pedersen
  • ,
  • Søren Bang Nielsen
  • ,
  • Daniel Otzen
The intrinsically disordered protein α-synuclein (αSN) is linked to Parkinson's Disease and forms both oligomeric species and amyloid fibrils. The N-terminal part of monomeric αSN interacts strongly with membranes and αSN cytotoxicity has been attributed to oligomers' ability to interact with and perturb membranes. We show that membrane folding of monomeric wt αSN and N-terminally truncated variants correlates with membrane permeabilization. Further, the first 11 N-terminal residues are crucial for monomers' and oligomers' interactions with and permeabilization of membranes. We attribute oligomer permeabilization both to cooperative electrostatic interactions through the N-terminus and interactions mediated by hydrophobic regions in the oligomer.
TidsskriftFEBS Letters
Sider (fra-til)497-502
Antal sider6
StatusUdgivet - 31 jan. 2014

Se relationer på Aarhus Universitet Citationsformater

ID: 68424261