Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates

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Standard

Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates. / Abelein, Axel; Kaspersen, Jørn Døvling; Nielsen, Søren Bang; Jensen, Grethe Vestergaard; Christiansen, Gunna; Pedersen, Jan Skov; Danielsson, Jens Albert; Otzen, Daniel; Gräslund, Astrid.

In: Journal of Biological Chemistry, Vol. 288, 09.08.2013, p. 23518-23528.

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

Harvard

Abelein, A, Kaspersen, JD, Nielsen, SB, Jensen, GV, Christiansen, G, Pedersen, JS, Danielsson, JA, Otzen, D & Gräslund, A 2013, 'Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates', Journal of Biological Chemistry, vol. 288, pp. 23518-23528. https://doi.org/10.1074/jbc.M113.470450

APA

Abelein, A., Kaspersen, J. D., Nielsen, S. B., Jensen, G. V., Christiansen, G., Pedersen, J. S., Danielsson, J. A., Otzen, D., & Gräslund, A. (2013). Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates. Journal of Biological Chemistry, 288, 23518-23528. https://doi.org/10.1074/jbc.M113.470450

CBE

Abelein A, Kaspersen JD, Nielsen SB, Jensen GV, Christiansen G, Pedersen JS, Danielsson JA, Otzen D, Gräslund A. 2013. Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates. Journal of Biological Chemistry. 288:23518-23528. https://doi.org/10.1074/jbc.M113.470450

MLA

Vancouver

Abelein A, Kaspersen JD, Nielsen SB, Jensen GV, Christiansen G, Pedersen JS et al. Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates. Journal of Biological Chemistry. 2013 Aug 9;288:23518-23528. https://doi.org/10.1074/jbc.M113.470450

Author

Abelein, Axel ; Kaspersen, Jørn Døvling ; Nielsen, Søren Bang ; Jensen, Grethe Vestergaard ; Christiansen, Gunna ; Pedersen, Jan Skov ; Danielsson, Jens Albert ; Otzen, Daniel ; Gräslund, Astrid. / Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates. In: Journal of Biological Chemistry. 2013 ; Vol. 288. pp. 23518-23528.

Bibtex

@article{a9989fc9bf6c416580c9b484eadad6d9,
title = "Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates",
abstract = "Intermediate amyloidogenic states along the amyloid β peptide (Aβ) aggregation pathway have been shown to be linked to neurotoxicity. To shed more light on the different structures that may arise during Aβ aggregation, we here investigate surfactant-induced Aβ aggregation. This process leads to co-aggregates featuring a β-structure motif that is characteristic for mature amyloid-like structures. Surfactants induce secondary structure in Aβ in a concentration-dependent manner, from predominantly random coil at low surfactant concentration, via β-structure to fully formed α-helical state at high surfactant concentration. The β-rich state is the most aggregation prone as monitored by Thioflavin T fluorescence. Small angle X-ray scattering reveals initial globular structures of surfactant-Aβ co-aggregated oligomers and formation of elongated fibrils during a slow aggregation process. Alongside this slow (min to h time scale) fibrillation process, much faster dynamic exchange (kex ~ 1100 s(-1)) takes place between free and co-aggregate-bound peptide. The two hydrophobic segments of the peptide are directly involved in the chemical exchange and interact with the hydrophobic part of the co-aggregates. Our findings suggest a model for surfactant-induced aggregation where free peptide and surfactant initially co-aggregate to dynamic globular oligomers and eventually form elongated fibrils. When interacting with β-structure promoting substances, such as surfactants, Aβ is kinetically driven towards an aggregation prone state.",
author = "Axel Abelein and Kaspersen, {J{\o}rn D{\o}vling} and Nielsen, {S{\o}ren Bang} and Jensen, {Grethe Vestergaard} and Gunna Christiansen and Pedersen, {Jan Skov} and Danielsson, {Jens Albert} and Daniel Otzen and Astrid Gr{\"a}slund",
year = "2013",
month = aug,
day = "9",
doi = "10.1074/jbc.M113.470450",
language = "English",
volume = "288",
pages = "23518--23528",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

}

RIS

TY - JOUR

T1 - Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates

AU - Abelein, Axel

AU - Kaspersen, Jørn Døvling

AU - Nielsen, Søren Bang

AU - Jensen, Grethe Vestergaard

AU - Christiansen, Gunna

AU - Pedersen, Jan Skov

AU - Danielsson, Jens Albert

AU - Otzen, Daniel

AU - Gräslund, Astrid

PY - 2013/8/9

Y1 - 2013/8/9

N2 - Intermediate amyloidogenic states along the amyloid β peptide (Aβ) aggregation pathway have been shown to be linked to neurotoxicity. To shed more light on the different structures that may arise during Aβ aggregation, we here investigate surfactant-induced Aβ aggregation. This process leads to co-aggregates featuring a β-structure motif that is characteristic for mature amyloid-like structures. Surfactants induce secondary structure in Aβ in a concentration-dependent manner, from predominantly random coil at low surfactant concentration, via β-structure to fully formed α-helical state at high surfactant concentration. The β-rich state is the most aggregation prone as monitored by Thioflavin T fluorescence. Small angle X-ray scattering reveals initial globular structures of surfactant-Aβ co-aggregated oligomers and formation of elongated fibrils during a slow aggregation process. Alongside this slow (min to h time scale) fibrillation process, much faster dynamic exchange (kex ~ 1100 s(-1)) takes place between free and co-aggregate-bound peptide. The two hydrophobic segments of the peptide are directly involved in the chemical exchange and interact with the hydrophobic part of the co-aggregates. Our findings suggest a model for surfactant-induced aggregation where free peptide and surfactant initially co-aggregate to dynamic globular oligomers and eventually form elongated fibrils. When interacting with β-structure promoting substances, such as surfactants, Aβ is kinetically driven towards an aggregation prone state.

AB - Intermediate amyloidogenic states along the amyloid β peptide (Aβ) aggregation pathway have been shown to be linked to neurotoxicity. To shed more light on the different structures that may arise during Aβ aggregation, we here investigate surfactant-induced Aβ aggregation. This process leads to co-aggregates featuring a β-structure motif that is characteristic for mature amyloid-like structures. Surfactants induce secondary structure in Aβ in a concentration-dependent manner, from predominantly random coil at low surfactant concentration, via β-structure to fully formed α-helical state at high surfactant concentration. The β-rich state is the most aggregation prone as monitored by Thioflavin T fluorescence. Small angle X-ray scattering reveals initial globular structures of surfactant-Aβ co-aggregated oligomers and formation of elongated fibrils during a slow aggregation process. Alongside this slow (min to h time scale) fibrillation process, much faster dynamic exchange (kex ~ 1100 s(-1)) takes place between free and co-aggregate-bound peptide. The two hydrophobic segments of the peptide are directly involved in the chemical exchange and interact with the hydrophobic part of the co-aggregates. Our findings suggest a model for surfactant-induced aggregation where free peptide and surfactant initially co-aggregate to dynamic globular oligomers and eventually form elongated fibrils. When interacting with β-structure promoting substances, such as surfactants, Aβ is kinetically driven towards an aggregation prone state.

U2 - 10.1074/jbc.M113.470450

DO - 10.1074/jbc.M113.470450

M3 - Journal article

C2 - 23775077

VL - 288

SP - 23518

EP - 23528

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -