Sökning: WFRF:(Jensen Grethe Vestergaard)
> (2013) >
Formation of dynami...
Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates
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- Abelein, Axel (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Kaspersen, Jørn Døvling (författare)
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Nielsen, Søren Bang (författare)
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Jensen, Grethe Vestergaard (författare)
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Christiansen, Gunna (författare)
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Pedersen, Jan Skov (författare)
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- Danielsson, Jens (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Otzen, Daniel E. (författare)
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- Gräslund, Astrid (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
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visa färre...
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(creator_code:org_t)
- 2013
- 2013
- Engelska.
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 288:32, s. 23518-23528
- Relaterad länk:
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https://doi.org/10.1...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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 the 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 (minutes to hours time scale) fibrillation process, much faster dynamic exchange (k(ex) ∼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 toward an aggregation-prone state.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Biophysics
- biofysik
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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