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Daniel Otzen

The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization

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The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. / Marvian, Amir Tayaranian; Aliakbari, Farhang; Mohammad-Beigi, Hossein et al.

In: International Journal of Biological Macromolecules, Vol. 155, 07.2020, p. 543-550.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Marvian, AT, Aliakbari, F, Mohammad-Beigi, H, Ahmadi, ZA, Mehrpouyan, S, Lermyte, F, Nasouti, M, Collingwood, JF, Otzen, DE & Morshedi, D 2020, 'The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization', International Journal of Biological Macromolecules, vol. 155, pp. 543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238

APA

Marvian, A. T., Aliakbari, F., Mohammad-Beigi, H., Ahmadi, Z. A., Mehrpouyan, S., Lermyte, F., Nasouti, M., Collingwood, J. F., Otzen, D. E., & Morshedi, D. (2020). The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules, 155, 543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238

CBE

Marvian AT, Aliakbari F, Mohammad-Beigi H, Ahmadi ZA, Mehrpouyan S, Lermyte F, Nasouti M, Collingwood JF, Otzen DE, Morshedi D. 2020. The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules. 155:543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238

MLA

Marvian, Amir Tayaranian et al. "The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization". International Journal of Biological Macromolecules. 2020, 155. 543-550. https://doi.org/10.1016/j.ijbiomac.2020.03.238

Vancouver

Marvian AT, Aliakbari F, Mohammad-Beigi H, Ahmadi ZA, Mehrpouyan S, Lermyte F et al. The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. International Journal of Biological Macromolecules. 2020 Jul;155:543-550. Epub 2020 Mar 30. doi: 10.1016/j.ijbiomac.2020.03.238

Author

Marvian, Amir Tayaranian ; Aliakbari, Farhang ; Mohammad-Beigi, Hossein et al. / The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization. In: International Journal of Biological Macromolecules. 2020 ; Vol. 155. pp. 543-550.

Bibtex

@article{4db2537f9b9f4ecf8740ba3531e9d387,
title = "The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization",
abstract = "The α-synuclein (αSN) amyloid fibrillization process is known to be a crucial phenomenon associated with neuronal loss in various neurodegenerative diseases, most famously Parkinson's disease. The process involves different aggregated species and ultimately leads to formation of β-sheet rich fibrillar structures. Despite the essential role of αSN aggregation in the pathoetiology of various neurological disorders, the characteristics of various assemblies are not fully understood. Here, we established a fluorescence-based model for studying the end-parts of αSN to decipher the structural aspects of aggregates during the fibrillization. Our model proved highly sensitive to the events at the early stage of the fibrillization process, which are hardly detectable with routine techniques. Combining fluorescent and PAGE analysis, we found different oligomeric aggregates in the nucleation phase of fibrillization with different sensitivity to SDS and different structures based on αSN termini. Moreover, we found that these oligomers are highly dynamic: after reaching peak levels during fibrillization, they decline and eventually disappear, suggesting their transformation into other αSN aggregated species. These findings shed light on the structural features of various αSN aggregates and their dynamics in synucleinopathies.",
keywords = "Alpha-Synuclein, Fibrillization, Fluorescence, Oligomer, Protein terminal labeling",
author = "Marvian, {Amir Tayaranian} and Farhang Aliakbari and Hossein Mohammad-Beigi and Ahmadi, {Zeinab Alsadat} and Sina Mehrpouyan and Frederik Lermyte and Mahour Nasouti and Collingwood, {Joanna F} and Otzen, {Daniel E} and Dina Morshedi",
note = "Copyright {\textcopyright} 2020. Published by Elsevier B.V.",
year = "2020",
month = jul,
doi = "10.1016/j.ijbiomac.2020.03.238",
language = "English",
volume = "155",
pages = "543--550",
journal = "International Journal of Biological Macromolecules",
issn = "0141-8130",
publisher = "Elsevier BV",

}

RIS

TY - JOUR

T1 - The status of the terminal regions of α-synuclein in different forms of aggregates during fibrillization

AU - Marvian, Amir Tayaranian

AU - Aliakbari, Farhang

AU - Mohammad-Beigi, Hossein

AU - Ahmadi, Zeinab Alsadat

AU - Mehrpouyan, Sina

AU - Lermyte, Frederik

AU - Nasouti, Mahour

AU - Collingwood, Joanna F

AU - Otzen, Daniel E

AU - Morshedi, Dina

N1 - Copyright © 2020. Published by Elsevier B.V.

PY - 2020/7

Y1 - 2020/7

N2 - The α-synuclein (αSN) amyloid fibrillization process is known to be a crucial phenomenon associated with neuronal loss in various neurodegenerative diseases, most famously Parkinson's disease. The process involves different aggregated species and ultimately leads to formation of β-sheet rich fibrillar structures. Despite the essential role of αSN aggregation in the pathoetiology of various neurological disorders, the characteristics of various assemblies are not fully understood. Here, we established a fluorescence-based model for studying the end-parts of αSN to decipher the structural aspects of aggregates during the fibrillization. Our model proved highly sensitive to the events at the early stage of the fibrillization process, which are hardly detectable with routine techniques. Combining fluorescent and PAGE analysis, we found different oligomeric aggregates in the nucleation phase of fibrillization with different sensitivity to SDS and different structures based on αSN termini. Moreover, we found that these oligomers are highly dynamic: after reaching peak levels during fibrillization, they decline and eventually disappear, suggesting their transformation into other αSN aggregated species. These findings shed light on the structural features of various αSN aggregates and their dynamics in synucleinopathies.

AB - The α-synuclein (αSN) amyloid fibrillization process is known to be a crucial phenomenon associated with neuronal loss in various neurodegenerative diseases, most famously Parkinson's disease. The process involves different aggregated species and ultimately leads to formation of β-sheet rich fibrillar structures. Despite the essential role of αSN aggregation in the pathoetiology of various neurological disorders, the characteristics of various assemblies are not fully understood. Here, we established a fluorescence-based model for studying the end-parts of αSN to decipher the structural aspects of aggregates during the fibrillization. Our model proved highly sensitive to the events at the early stage of the fibrillization process, which are hardly detectable with routine techniques. Combining fluorescent and PAGE analysis, we found different oligomeric aggregates in the nucleation phase of fibrillization with different sensitivity to SDS and different structures based on αSN termini. Moreover, we found that these oligomers are highly dynamic: after reaching peak levels during fibrillization, they decline and eventually disappear, suggesting their transformation into other αSN aggregated species. These findings shed light on the structural features of various αSN aggregates and their dynamics in synucleinopathies.

KW - Alpha-Synuclein

KW - Fibrillization

KW - Fluorescence

KW - Oligomer

KW - Protein terminal labeling

U2 - 10.1016/j.ijbiomac.2020.03.238

DO - 10.1016/j.ijbiomac.2020.03.238

M3 - Journal article

C2 - 32240735

VL - 155

SP - 543

EP - 550

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

SN - 0141-8130

ER -