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タイトル: | Cyclodextrin-responsive nanogel as an artificial chaperone for horseradish peroxidase |
著者: | Sawada, Shin-ichi Sasaki, Yoshihiro Nomura, Yuta Akiyoshi, Kazunari ![]() ![]() |
著者名の別形: | 澤田, 晋一 秋吉, 一成 |
キーワード: | Artificial chaperone Protein refolding Nanogel Hydrophobic interaction Cyclodextrin |
発行日: | Apr-2011 |
出版者: | Springer-Verlag |
誌名: | Colloid and Polymer Science |
巻: | 289 |
号: | 5-6 |
開始ページ: | 685 |
終了ページ: | 691 |
記述: | The thermal stabilization and refolding of horseradish peroxidase (HRP) upon heating were investigated using an artificial molecular chaperone consisting of cholesterol-bearing pullulan (CHP) nanogels. The CHP nanogels inhibited the aggregation of HRP under heating by complexation with the denatured HRP. The enzyme activity of HRP complexed with CHP nanogels was not detected. However, the enzyme activity recovered up to 80% of native HRP after the addition of cyclodextrin (CD) to the complex. The dissociation of CHP nanogels was induced by the formation of an inclusion complex of cholesterol groups of CHP with CD. The enzyme activity of HRP was only significantly recovered by the addition of β-CD or its derivatives. Natural molecular chaperones, such as GroEL/ES, trap, fold, and release the nonnative proteins by changing the hydrophobicity of the specific sites of the molecular chaperone that interact with the nonnative protein. The functional mechanism of the nanogel chaperon system is similar to that of natural molecular chaperones. The nanogel chaperone system is a useful tool to aid the refolding and thermal stabilization of unstable proteins for post-genome research, and in medical and biological applications. |
著作権等: | The final publication is available at www.springerlink.com This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 |
URI: | http://hdl.handle.net/2433/143599 |
DOI(出版社版): | 10.1007/s00396-010-2361-0 |
出現コレクション: | 学術雑誌掲載論文等 |

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