Abstract：
:The conversion of α-synuclein from its natively unfolded and α-helical tetrameric forms to an amyloid conformation is central to the emergence of Parkinson's disease. Therefore, prevention of this conversion may offer an effective way of avoiding the onset of this disease or delaying its progress. At different concentrations, an aqueous extract from the edible winged kelp (Alaria esculenta), was shown to lower and to raise the melting point of α-synuclein. Size fractionation of the extract resulted in the separation of these distinct activities. The fraction below 5kDa decreased the melting point of α-synuclein, whereas the fraction above 10kDa raised the melting point. Both of these fractions were found to inhibit the formation of amyloid aggregates by α-synuclein, measured by thioflavin T dye-binding assays; this effect was further confirmed by transmission electron microscopy showing the inhibition of fibril formation. Circular dichroism analysis suggested that the incubation of α-synuclein under fibrillation conditions resulted in the loss of substantial native helical structure in the presence and absence of the fractions. It is therefore likely that the fractions inhibit fibrillation by interacting with the unfolded form of α-synuclein.
journal_name
Neurosci Lettjournal_title
Neuroscience lettersauthors
Giffin JC,Richards RC,Craft C,Jahan N,Leggiadro C,Chopin T,Szemerda M,MacKinnon SL,Ewart KVdoi
10.1016/j.neulet.2017.02.055subject
Has Abstractpub_date
2017-03-22 00:00:00pages
87-93eissn
0304-3940issn
1872-7972pii
S0304-3940(17)30171-4journal_volume
644pub_type
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