Electron microscopic study of the effect of fullerene on the formation of amyloid fibrils by the Aβ25-35 peptide

被引：7
|
作者：
Podlubnaya Z.A. [1 ,2 ]
Podol'Skii I.Ya. [1 ,2 ]
Shpagina M.D. [1 ]
Marsagishvili L.G. [1 ]
机构：
[1] Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region
[2] Pushchino State University, Pushchino, Moscow Region
来源：
Biophysics | 2006年 / 51卷 / 5期
基金：
俄罗斯基础研究基金会;
关键词：
Aβ[!sub]25-35[!/sub; Alzheimer's disease; Amyloidoses; Amyloids; Electron microscopy; Fullerene;
D O I：
10.1134/S0006350906050046
中图分类号：
学科分类号：
摘要：
The antiamyloidogenic effect of hydrated fullerence C60 HyFn was shown by electron microscopy. It was found that fullerene binds to growing fibrils formed by the [beta]-amyloid peptide Aβ25-35 and thus prevents their further growth and interferes with the formation of new fibrils. Instead of long broad helically twisted 'ribbons' formed by Aβ 25-35 in the absence of fullerene, short narrow protofibrils form in its presence. These results suggest that fullerenes can be useful in treatment for Alzheimer's disease. © Nauka/Interperiodica 2006.
引用
收藏
页码：701 / 704
页数：3
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