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このアイテムの引用には次の識別子を使用してください:
http://hdl.handle.net/10119/13537
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| タイトル: | A zwitterionic polymer as a novel inhibitor of protein aggregation |
| 著者: | Rajan, Robin
Matsumura, Kazuaki |
| 発行日: | 2015-06-19 |
| 出版者: | Royal Society of Chemistry |
| 誌名: | Journal of Materials Chemistry B |
| 巻: | 3 |
| 号: | 28 |
| 開始ページ: | 5683 |
| 終了ページ: | 5689 |
| DOI: | 10.1039/C5TB01021G |
| 抄録: | We report the novel one-step synthesis of a zwitterionic polymer, poly-sulfobetaine, via living reversible addition fragmentation chain transfer (RAFT) polymerization. Lysozyme did not aggregate when heated in presence of this polymer. Amyloid formation, the cause of many diseases, was also suppressed. The zwitterionic polymer was significantly more efficient than previously described inhibitors of protein aggregation. Lysozyme heated in the presence of polysulfobetaine retained its solubility and very high enzymatic efficiency, even after prolonged heating. The secondary structures of lysozyme change with increasing temperature, accompanied by an increase in β-structure. This change was prevented by mixing the polymer with lysozyme. ^1H-NMR before and after aggregation revealed the conformational changes taking place in the lysozyme: during aggregation, lysozyme is transformed into a random coil conformation, thus losing its secondary structure. Presence of the polymer facilitates retention of partial higher order structures and lysozyme solubility at higher temperatures. The high efficiency of the polyampholyte was ascribed to its ability to prevent collisions between aggregating species by acting as molecular shield. |
| Rights: | Copyright (C) 2015 Royal Society of Chemistry. Robin Rajan and Kazuaki Matsumura, Journal of Materials Chemistry B, 3(28), 2015, 5683-5689. http://dx.doi.org/10.1039/C5TB01021G - Reproduced by permission of The Royal Society of Chemistry |
| URI: | http://hdl.handle.net/10119/13537 |
| 資料タイプ: | author |
| 出現コレクション: | c10-1. 雑誌掲載論文 (Journal Articles)
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