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Suppression of amyloid fibrils using the GroEL apical domain
https://repository.lib.tottori-u.ac.jp/records/7369
https://repository.lib.tottori-u.ac.jp/records/7369df4085a8-d959-4ab7-b100-c56b9a3ff342
| 名前 / ファイル | ライセンス | アクション |
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sr_srep31041.pdf (5.7 MB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2022-06-30 | |||||
| タイトル | ||||||
| タイトル | Suppression of amyloid fibrils using the GroEL apical domain | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ | journal article | |||||
| 著者 |
本郷, 邦広
× 本郷, 邦広× 溝端, 知宏× 河田, 康志× Ojha, Bimlesh× Fukui, Naoya |
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| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University | |||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University | |||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University | |||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University | |||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Department of Chemistry and Biotechnology, Graduate School of Engineering Tottori University / Department of Biomedical Science, Institute of Regenerative Medicine and Biofunction, Graduate School of Medical Science, Tottori University | |||||
| 抄録 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | In E. coli cells, rescue of non-native proteins and promotion of native state structure is assisted by the chaperonin GroEL. An important key to this activity lies in the structure of the apical domain of GroEL (GroEL-AD) (residue 191–376), which recognizes and binds non-native protein molecules through hydrophobic interactions. In this study, we investigated the effects of GroEL-AD on the aggregation of various client proteins (α-Synuclein, Aβ42, and GroES) that lead to the formation of distinct protein fibrils in vitro. We found that GroEL-AD effectively inhibited the fibril formation of these three proteins when added at concentrations above a critical threshold; the specific ratio differed for each client protein, reflecting the relative affinities. The effect of GroEL-AD in all three cases was to decrease the concentration of aggregate-forming unfolded client protein or its early intermediates in solution, thereby preventing aggregation and fibrillation. Binding affinity assays revealed some differences in the binding mechanisms of GroEL-AD toward each client. Our findings suggest a possible applicability of this minimal functioning derivative of the chaperonins (the “minichaperones”) as protein fibrillation modulators and detectors. | |||||
| 書誌情報 |
Scientific Reports en : Scientific Reports 巻 6, 発行日 2016-08-04 |
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| 出版者 | ||||||
| 出版者 | Springer Nature | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 20452322 | |||||
| DOI | ||||||
| 関連タイプ | isIdenticalTo | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1038/srep31041 | |||||
| 権利 | ||||||
| 権利情報 | (C) The Author(s) 2016. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in th | |||||
| 情報源 | ||||||
| 関連名称 | Ojha Bimlesh, Fukui Naoya, Hongo Kunihiro, et al. Suppression of amyloid fibrils using the GroEL apical domain. Scientific Reports. 2016. 6. doi:10.1038/srep31041 | |||||
| 関連サイト | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | https://www.nature.com/articles/srep31041 | |||||
| 関連名称 | https://www.nature.com/articles/srep31041 | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
