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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 avis › Tidsskriftartikel › Forskning › peer review

DOI

  • 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.
OriginalsprogEngelsk
TidsskriftFEBS Letters
Vol/bind588
Nummer3
Sider (fra-til)497-502
Antal sider6
ISSN0014-5793
DOI
StatusUdgivet - 31 jan. 2014

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