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

被引：0
|
作者：
Podlubnaya, Z. A. [1 ]
Podolski, I. Ya.
Shpagina, M. D.
Marsagishvili, L. G.
机构：
[1] Russian Acad Sci, Inst Theoret & Expt Biophys, Pushchino 142290, Moscow Region, Russia
[2] Pushchino State Univ, Pushchino 142290, Moscow Region, Russia
来源：
BIOFIZIKA | 2006年 / 51卷 / 05期
关键词：
amyloids; amyloidoses; Alzheimer's disease; A beta(25-35)-peptide; fullerenes; electron microscopy;
D O I：
暂无
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
The anti-amyloidogenic capacity of hydrated fullerene C-60 HyFn was revealed by the use of electron microscopy. We first showed that when, connecting with growing amyloid fibrils formed by A beta(25-35)-peptide, fullerene prevented their subsequent growth and interfered with the formation of new fibrils. Instead of long helically twisted ribbons formed by A beta(25-35)-PePtide in the absence of fullerene, short narrow protofibrils were found in the presence of fullerene. These results allow one to suppose that fullerene can be useful for the therapy of Alzheimer's disease.
引用
收藏
页码：795 / 798
页数：4
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