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タイトル: | Anti-prion activity of an RNA aptamer and its structural basis. |
著者: | Mashima, Tsukasa Nishikawa, Fumiko Kamatari, Yuji O Fujiwara, Hiromichi Saimura, Masayuki Nagata, Takashi https://orcid.org/0000-0002-3733-2709 (unconfirmed) Kodaki, Tsutomu Nishikawa, Satoshi Kuwata, Kazuo Katahira, Masato https://orcid.org/0000-0003-0336-7660 (unconfirmed) |
著者名の別形: | 片平, 正人 |
発行日: | Jan-2013 |
出版者: | Oxford University Press |
誌名: | Nucleic acids research |
巻: | 41 |
号: | 2 |
開始ページ: | 1355 |
終了ページ: | 1362 |
抄録: | Prion proteins (PrPs) cause prion diseases, such as bovine spongiform encephalopathy. The conversion of a normal cellular form (PrP(C)) of PrP into an abnormal form (PrP(Sc)) is thought to be associated with the pathogenesis. An RNA aptamer that tightly binds to and stabilizes PrP(C) is expected to block this conversion and to thereby prevent prion diseases. Here, we show that an RNA aptamer comprising only 12 residues, r(GGAGGAGGAGGA) (R12), reduces the PrP(Sc) level in mouse neuronal cells persistently infected with the transmissible spongiform encephalopathy agent. Nuclear magnetic resonance analysis revealed that R12, folded into a unique quadruplex structure, forms a dimer and that each monomer simultaneously binds to two portions of the N-terminal half of PrP(C), resulting in tight binding. Electrostatic and stacking interactions contribute to the affinity of each portion. Our results demonstrate the therapeutic potential of an RNA aptamer as to prion diseases. |
著作権等: | © The Author(s) 2012. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial reuse, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com. |
URI: | http://hdl.handle.net/2433/173326 |
DOI(出版社版): | 10.1093/nar/gks1132 |
PubMed ID: | 23180780 |
出現コレクション: | 学術雑誌掲載論文等 |
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