Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils

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

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Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils. / Brown, James W P; Meisl, Georg; Knowles, Tuomas P J; Buell, Alexander K; Dobson, Christopher M; Galvagnion, Céline.

In: Chemical communications (Cambridge, England), Vol. 54, No. 56, 10.07.2018, p. 7854-7857.

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

Harvard

Brown, JWP, Meisl, G, Knowles, TPJ, Buell, AK, Dobson, CM & Galvagnion, C 2018, 'Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils', Chemical communications (Cambridge, England), vol. 54, no. 56, pp. 7854-7857. https://doi.org/10.1039/c8cc03002b

APA

Brown, J. W. P., Meisl, G., Knowles, T. P. J., Buell, A. K., Dobson, C. M., & Galvagnion, C. (2018). Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils. Chemical communications (Cambridge, England), 54(56), 7854-7857. https://doi.org/10.1039/c8cc03002b

Vancouver

Brown JWP, Meisl G, Knowles TPJ, Buell AK, Dobson CM, Galvagnion C. Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils. Chemical communications (Cambridge, England). 2018 Jul 10;54(56):7854-7857. https://doi.org/10.1039/c8cc03002b

Author

Brown, James W P ; Meisl, Georg ; Knowles, Tuomas P J ; Buell, Alexander K ; Dobson, Christopher M ; Galvagnion, Céline. / Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils. In: Chemical communications (Cambridge, England). 2018 ; Vol. 54, No. 56. pp. 7854-7857.

Bibtex

@article{964926e01b3c4c34a7c406f5088d027b,
title = "Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils",
abstract = "Oligomeric and protofibrillar aggregates that are populated along the pathway of amyloid fibril formation appear generally to be more toxic than the mature fibrillar state. In particular, α-synuclein, the protein associated with Parkinson's disease, forms kinetically trapped protofibrils in the presence of lipid vesicles. Here, we show that lipid-induced α-synuclein protofibrils can convert rapidly to mature fibrils at higher temperatures. Furthermore, we find that β-synuclein, generally considered less aggregation prone than α-synuclein, forms protofibrils at higher temperatures. These findings highlight the importance of energy barriers in controlling the de novo formation and conversion of amyloid fibrils.",
author = "Brown, {James W P} and Georg Meisl and Knowles, {Tuomas P J} and Buell, {Alexander K} and Dobson, {Christopher M} and C{\'e}line Galvagnion",
year = "2018",
month = jul,
day = "10",
doi = "10.1039/c8cc03002b",
language = "English",
volume = "54",
pages = "7854--7857",
journal = "Chemical Communications",
issn = "1359-7345",
publisher = "Royal Society of Chemistry",
number = "56",

}

RIS

TY - JOUR

T1 - Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils

AU - Brown, James W P

AU - Meisl, Georg

AU - Knowles, Tuomas P J

AU - Buell, Alexander K

AU - Dobson, Christopher M

AU - Galvagnion, Céline

PY - 2018/7/10

Y1 - 2018/7/10

N2 - Oligomeric and protofibrillar aggregates that are populated along the pathway of amyloid fibril formation appear generally to be more toxic than the mature fibrillar state. In particular, α-synuclein, the protein associated with Parkinson's disease, forms kinetically trapped protofibrils in the presence of lipid vesicles. Here, we show that lipid-induced α-synuclein protofibrils can convert rapidly to mature fibrils at higher temperatures. Furthermore, we find that β-synuclein, generally considered less aggregation prone than α-synuclein, forms protofibrils at higher temperatures. These findings highlight the importance of energy barriers in controlling the de novo formation and conversion of amyloid fibrils.

AB - Oligomeric and protofibrillar aggregates that are populated along the pathway of amyloid fibril formation appear generally to be more toxic than the mature fibrillar state. In particular, α-synuclein, the protein associated with Parkinson's disease, forms kinetically trapped protofibrils in the presence of lipid vesicles. Here, we show that lipid-induced α-synuclein protofibrils can convert rapidly to mature fibrils at higher temperatures. Furthermore, we find that β-synuclein, generally considered less aggregation prone than α-synuclein, forms protofibrils at higher temperatures. These findings highlight the importance of energy barriers in controlling the de novo formation and conversion of amyloid fibrils.

U2 - 10.1039/c8cc03002b

DO - 10.1039/c8cc03002b

M3 - Journal article

C2 - 29951679

VL - 54

SP - 7854

EP - 7857

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 56

ER -

ID: 216263040