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

Abelein, Axel (author)
Stockholms universitet,Institutionen för biokemi och biofysik
Kaspersen, Jørn Døvling (author)
Nielsen, Søren Bang (author)
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Jensen, Grethe Vestergaard (author)
Christiansen, Gunna (author)
Pedersen, Jan Skov (author)
Danielsson, Jens (author)
Stockholms universitet,Institutionen för biokemi och biofysik
Otzen, Daniel E. (author)
Gräslund, Astrid (author)
Stockholms universitet,Institutionen för biokemi och biofysik
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 (creator_code:org_t)
2013
2013
English.
In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 288:32, s. 23518-23528
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  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

Biophysics
biofysik

Publication and Content Type

ref (subject category)
art (subject category)

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