A.N. Bach Institute of Biochemistry, The Russian Academy of Sciences, Moscow, Russia.
Prion. 2012 Sep-Oct;6(4):400-6. doi: 10.4161/pri.20678. Epub 2012 Aug 9.
Amyloids are fibrillar protein aggregates resulting from non-covalent autocatalytic polymerization of various structurally and functionally unrelated proteins. Previously we have selected DNA aptamers, which bind specifically to the in vitro assembled amyloid fibrils of the yeast prionogenic protein Sup35. Here we show that such DNA aptamers can be used to detect SDS-insoluble amyloid aggregates of the Sup35 protein, and of some other amyloidogenic proteins, including mouse PrP, formed in yeast cells. The obtained data suggest that these aggregates and the Sup35 amyloid fibrils assembled in vitro possess common conformational epitopes recognizable by aptamers. The described DNA aptamers may be used for detection of various amyloid aggregates in yeast and, presumably, other organisms.
淀粉样物是由各种结构和功能上不相关的蛋白质非共价自动催化聚合而成的纤维状蛋白聚集体。之前我们已经选择了 DNA 适体，它可以特异性地结合酵母朊病毒蛋白 Sup35 的体外组装淀粉样纤维。在这里，我们表明，这些 DNA 适体可用于检测酵母细胞中 Sup35 蛋白以及其他一些淀粉样蛋白形成的 SDS 不溶性淀粉样聚集物。所得数据表明，这些聚集物和体外组装的 Sup35 淀粉样纤维具有共同的构象表位，可被适体识别。所描述的 DNA 适体可用于检测酵母中的各种淀粉样聚集物，并且推测也可用于其他生物体。
