Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo, 184-8588, Japan.
Biotechnol Lett. 2010 May;32(5):643-8. doi: 10.1007/s10529-010-0200-5. Epub 2010 Jan 29.
Alpha-synuclein is a native, unfolded protein that causes several neurodegenerative diseases such as dementia with Lewy bodies and Parkinson's disease. We have now identified the first DNA aptamers against alpha-synuclein using native PAGE applied to the SELEX method. We call this aptamer "M5-15"; it is the alpha-synuclein-bound aptamer and was isolated after four cycles of screening. M5-15 is composed of three stem-loop structures that may play an important role in the binding to alpha-synuclein. Moreover, M5-15 specifically binds to the alpha-synuclein monomer and oligomer. We expect that this aptamer will become a useful tool in alpha-synuclein analysis and diagnosis.
α-突触核蛋白是一种天然的、未折叠的蛋白质，可导致几种神经退行性疾病，如路易体痴呆和帕金森病。我们现在已经使用应用于 SELEX 方法的天然 PAGE 鉴定了针对 α-突触核蛋白的第一个 DNA 适体。我们将这个适体称为“M5-15”；它是与 α-突触核蛋白结合的适体，是经过四轮筛选后分离得到的。M5-15 由三个茎环结构组成，这些结构可能在与 α-突触核蛋白结合中发挥重要作用。此外，M5-15 特异性结合于 α-突触核蛋白单体和寡聚物。我们期望这个适体将成为 α-突触核蛋白分析和诊断的有用工具。
