科研之友
微信
新浪微博
Facebook
分享链接
摘要
The conversion of alpha-synuclein from its natively unfolded and alpha-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 alpha-synuclein. Size fractionation of the extract resulted in the separation of these distinct activities. The fraction below 5 kDa decreased the melting point of alpha-synuclein, whereas the fraction above 10 kDa raised the melting point. Both of these fractions were found to inhibit the formation of amyloid aggregates by alpha-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 alpha-synuclein under fibrillation conditions resulted in the loss of substantial native helical structure in the presence and absence of the fraction. It is therefore likely that the fractions inhibit fibrillation by interacting with the unfolded form of alpha-synuclein.
- 出版日期2017-3-22
