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聚-L-谷氨酸淀粉样蛋白形成一种新型超分子结构。

The formation of a novel supramolecular structure by amyloid of poly-L-glutamic acid.

作者信息

Bai Fan, Zeng Chengming, Yang Shixin, Zhang Yizheng, He Yi, Jin Jun

机构信息

College of Life Science, Sichuan University, Sichuan Key Laboratory of Molecular Biology & Biotechnology, No. 29, Wangjiang Road, Chengdu 610064, People's Republic of China.

出版信息

Biochem Biophys Res Commun. 2008 May 9;369(3):830-4. doi: 10.1016/j.bbrc.2008.02.085. Epub 2008 Feb 26.

Abstract

Polyglutamic acid (PE) has been shown to form amyloid fibrils in vitro under pH value of 4.0. However, under the pH of 2.0, a further self-association process resulting in a novel supramolecular structure was observed. These supramolecular assemblies had diameters ranging from 1 to 20 microm and lengths up to several hundred microns, which were significantly larger than those of typical "amyloid fibrils". The existence of amyloid-like structure within these assemblies was confirmed with Fourier transform infrared spectroscopy and Thioflavin T fluorescence assay. The aggregation process of PE was studied by direct observation of electronic microscopy. The supramolecular assemblies appeared to be formed in a hierarchical process in which the preformed amyloid-like subunits self-assembled into higher-order assemblies in a well-organized pattern.

摘要

聚谷氨酸(PE)已被证明在体外pH值为4.0的条件下会形成淀粉样原纤维。然而,在pH值为2.0时,观察到了进一步的自组装过程,形成了一种新型超分子结构。这些超分子聚集体的直径范围为1至20微米,长度可达数百微米,明显大于典型的“淀粉样原纤维”。通过傅里叶变换红外光谱和硫黄素T荧光测定法证实了这些聚集体中存在类淀粉样结构。通过电子显微镜直接观察研究了PE的聚集过程。超分子聚集体似乎是通过分级过程形成的,其中预先形成的类淀粉样亚基以有序的模式自组装成更高阶的聚集体。

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