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

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The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes. / Lorenzen, Nikolai; Lemminger, Lasse; Pedersen, Jannik Nedergaard; Nielsen, Søren Bang; Otzen, Daniel.

In: FEBS Letters, Vol. 588, No. 3, 31.01.2014, p. 497-502.

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Lorenzen, Nikolai ; Lemminger, Lasse ; Pedersen, Jannik Nedergaard ; Nielsen, Søren Bang ; Otzen, Daniel. / The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes. In: FEBS Letters. 2014 ; Vol. 588, No. 3. pp. 497-502.

Bibtex

@article{908c42a2e2ae429fabc10f8a6f6b7607,
title = "The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes",
abstract = "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.",
author = "Nikolai Lorenzen and Lasse Lemminger and Pedersen, {Jannik Nedergaard} and Nielsen, {S{\o}ren Bang} and Daniel Otzen",
note = "Copyright {\textcopyright} 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",
year = "2014",
month = jan,
day = "31",
doi = "10.1016/j.febslet.2013.12.015",
language = "English",
volume = "588",
pages = "497--502",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd.",
number = "3",

}

RIS

TY - JOUR

T1 - The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes

AU - Lorenzen, Nikolai

AU - Lemminger, Lasse

AU - Pedersen, Jannik Nedergaard

AU - Nielsen, Søren Bang

AU - Otzen, Daniel

N1 - Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

PY - 2014/1/31

Y1 - 2014/1/31

N2 - 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.

AB - 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.

U2 - 10.1016/j.febslet.2013.12.015

DO - 10.1016/j.febslet.2013.12.015

M3 - Journal article

C2 - 24374342

VL - 588

SP - 497

EP - 502

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 3

ER -