Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation. / Galvagnion, Celine; Buell, Alexander K.; Meisl, Georg; Michaels, Thomas C. T.; Vendruscolo, Michele; Knowles, Tuomas P. J.; Dobson, Christopher M.

In: Nature Chemical Biology, Vol. 11, No. 3, 03.2015, p. 229-U101.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Galvagnion, C, Buell, AK, Meisl, G, Michaels, TCT, Vendruscolo, M, Knowles, TPJ & Dobson, CM 2015, 'Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation', Nature Chemical Biology, vol. 11, no. 3, pp. 229-U101. https://doi.org/10.1038/NCHEMBIO.1750

APA

Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015). Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation. Nature Chemical Biology, 11(3), 229-U101. https://doi.org/10.1038/NCHEMBIO.1750

Vancouver

Galvagnion C, Buell AK, Meisl G, Michaels TCT, Vendruscolo M, Knowles TPJ et al. Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation. Nature Chemical Biology. 2015 Mar;11(3):229-U101. https://doi.org/10.1038/NCHEMBIO.1750

Author

Galvagnion, Celine ; Buell, Alexander K. ; Meisl, Georg ; Michaels, Thomas C. T. ; Vendruscolo, Michele ; Knowles, Tuomas P. J. ; Dobson, Christopher M. / Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation. In: Nature Chemical Biology. 2015 ; Vol. 11, No. 3. pp. 229-U101.

Bibtex

@article{e7b7237574414df4bfc98ab6583fe842,
title = "Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation",
abstract = "α-Synuclein (α-syn) is a 140-residue intrinsically disordered protein that is involved in neuronal and synaptic vesicle plasticity, but its aggregation to form amyloid fibrils is the hallmark of Parkinson's disease (PD). The interaction between α-syn and lipid surfaces is believed to be a key feature for mediation of its normal function, but under other circumstances it is able to modulate amyloid fibril formation. Using a combination of experimental and theoretical approaches, we identify the mechanism through which facile aggregation of α-syn is induced under conditions where it binds a lipid bilayer, and we show that the rate of primary nucleation can be enhanced by three orders of magnitude or more under such conditions. These results reveal the key role that membrane interactions can have in triggering conversion of α-syn from its soluble state to the aggregated state that is associated with neurodegeneration and to its associated disease states.",
author = "Celine Galvagnion and Buell, {Alexander K.} and Georg Meisl and Michaels, {Thomas C. T.} and Michele Vendruscolo and Knowles, {Tuomas P. J.} and Dobson, {Christopher M.}",
year = "2015",
month = mar,
doi = "10.1038/NCHEMBIO.1750",
language = "English",
volume = "11",
pages = "229--U101",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "nature publishing group",
number = "3",

}

RIS

TY - JOUR

T1 - Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation

AU - Galvagnion, Celine

AU - Buell, Alexander K.

AU - Meisl, Georg

AU - Michaels, Thomas C. T.

AU - Vendruscolo, Michele

AU - Knowles, Tuomas P. J.

AU - Dobson, Christopher M.

PY - 2015/3

Y1 - 2015/3

N2 - α-Synuclein (α-syn) is a 140-residue intrinsically disordered protein that is involved in neuronal and synaptic vesicle plasticity, but its aggregation to form amyloid fibrils is the hallmark of Parkinson's disease (PD). The interaction between α-syn and lipid surfaces is believed to be a key feature for mediation of its normal function, but under other circumstances it is able to modulate amyloid fibril formation. Using a combination of experimental and theoretical approaches, we identify the mechanism through which facile aggregation of α-syn is induced under conditions where it binds a lipid bilayer, and we show that the rate of primary nucleation can be enhanced by three orders of magnitude or more under such conditions. These results reveal the key role that membrane interactions can have in triggering conversion of α-syn from its soluble state to the aggregated state that is associated with neurodegeneration and to its associated disease states.

AB - α-Synuclein (α-syn) is a 140-residue intrinsically disordered protein that is involved in neuronal and synaptic vesicle plasticity, but its aggregation to form amyloid fibrils is the hallmark of Parkinson's disease (PD). The interaction between α-syn and lipid surfaces is believed to be a key feature for mediation of its normal function, but under other circumstances it is able to modulate amyloid fibril formation. Using a combination of experimental and theoretical approaches, we identify the mechanism through which facile aggregation of α-syn is induced under conditions where it binds a lipid bilayer, and we show that the rate of primary nucleation can be enhanced by three orders of magnitude or more under such conditions. These results reveal the key role that membrane interactions can have in triggering conversion of α-syn from its soluble state to the aggregated state that is associated with neurodegeneration and to its associated disease states.

U2 - 10.1038/NCHEMBIO.1750

DO - 10.1038/NCHEMBIO.1750

M3 - Journal article

VL - 11

SP - 229-U101

JO - Nature Chemical Biology

JF - Nature Chemical Biology

SN - 1552-4450

IS - 3

ER -

ID: 216265021