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

Axel Abelein; Jørn Døvling Kaspersen; Søren Bang Nielsen; Grethe Vestergaard Jensen; Gunna Christiansen; Jan Skov Pedersen; Jens Danielsson; Daniel E. Otzen; Astrid Gräslund

doi:10.1074/jbc.M113.470450

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

Axel Abelein, Jørn Døvling Kaspersen, Søren Bang Nielsen, Grethe Vestergaard Jensen, Gunna Christiansen, Jan Skov Pedersen, Jens Danielsson, Daniel E. Otzen, Astrid Gräslund^*

^*Kontaktforfatter

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

42 Citationer (Scopus)

Abstract

Background: β-Structured oligomers of the amyloid β peptide are considered neurotoxic and on-pathway to amyloid fibril formation. Results: Surfactant-induced co-aggregated oligomers show dynamic rapid exchange with free peptide during a slow fibril formation process. Conclusion: β-Structure inducing small molecules kinetically promote peptide assembly into co-aggregates. Significance: Knowledge about molecular mechanisms of peptide aggregation modulators is potentially helpful for therapeutic purposes.

Originalsprog	Engelsk
Tidsskrift	Journal of Biological Chemistry
Vol/bind	288
Udgave nummer	32
Sider (fra-til)	23518-23528
Antal sider	11
ISSN	0021-9258
DOI	https://doi.org/10.1074/jbc.M113.470450
Status	Udgivet - 9 aug. 2013
Udgivet eksternt	Ja

Bibliografisk note

Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.

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10.1074/jbc.M113.470450

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title = "Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates",

abstract = "Background: β-Structured oligomers of the amyloid β peptide are considered neurotoxic and on-pathway to amyloid fibril formation. Results: Surfactant-induced co-aggregated oligomers show dynamic rapid exchange with free peptide during a slow fibril formation process. Conclusion: β-Structure inducing small molecules kinetically promote peptide assembly into co-aggregates. Significance: Knowledge about molecular mechanisms of peptide aggregation modulators is potentially helpful for therapeutic purposes.",

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doi = "10.1074/jbc.M113.470450",

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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

AU - Otzen, Daniel E.

AU - Gräslund, Astrid

PY - 2013/8/9

Y1 - 2013/8/9

N2 - Background: β-Structured oligomers of the amyloid β peptide are considered neurotoxic and on-pathway to amyloid fibril formation. Results: Surfactant-induced co-aggregated oligomers show dynamic rapid exchange with free peptide during a slow fibril formation process. Conclusion: β-Structure inducing small molecules kinetically promote peptide assembly into co-aggregates. Significance: Knowledge about molecular mechanisms of peptide aggregation modulators is potentially helpful for therapeutic purposes.

AB - Background: β-Structured oligomers of the amyloid β peptide are considered neurotoxic and on-pathway to amyloid fibril formation. Results: Surfactant-induced co-aggregated oligomers show dynamic rapid exchange with free peptide during a slow fibril formation process. Conclusion: β-Structure inducing small molecules kinetically promote peptide assembly into co-aggregates. Significance: Knowledge about molecular mechanisms of peptide aggregation modulators is potentially helpful for therapeutic purposes.

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U2 - 10.1074/jbc.M113.470450

DO - 10.1074/jbc.M113.470450

M3 - Journal article

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SN - 0021-9258

VL - 288

SP - 23518

EP - 23528

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 32

ER -

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

Abstract

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