The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes
In: FEBS letters, Jg. 588 (2013-10-22), Heft 3, S. 497-502
Online
unknown
Zugriff:
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.
Titel: |
The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes
|
---|---|
Autor/in / Beteiligte Person: | Lorenzen, Nikolai ; Otzen, Daniel E. ; Nielsen, Søren B. ; Lemminger, Lasse ; Jannik Nedergaard Pedersen |
Link: | |
Zeitschrift: | FEBS letters, Jg. 588 (2013-10-22), Heft 3, S. 497-502 |
Veröffentlichung: | 2013 |
Medientyp: | unknown |
ISSN: | 1873-3468 (print) |
Schlagwort: |
|
Sonstiges: |
|