| アイテムタイプ |
文献 / Documents(1) |
| 公開日 |
2026-04-09 |
| アクセス権 |
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アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 出版社版DOI |
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関連識別子 |
https://doi.org/10.1039/D4SC02123A |
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関連名称 |
10.1039/D4SC02123A |
| 出版タイプ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| タイトル |
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タイトル |
Redox-active chemical chaperones exhibiting promiscuous binding promote oxidative protein folding under condensed sub-millimolar conditions |
| 著者 |
Suzuki, Koki
Nojiri, Ryoya
松﨑, 元紀
Mabuchi, Takuya
Kanemura, Shingo
Ishii, Kotone
Kumeta, Hiroyuki
Okumura, Masaki
齋尾, 智英
Muraoka, Takahiro
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| 抄録 |
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内容記述 |
Proteins form native structures through folding processes, many of which proceed through intramolecular hydrophobic effect, hydrogen bond and disulfide-bond formation. In vivo, protein aggregation is prevented even in the highly condensed milieu of a cell through folding mediated by molecular chaperones and oxidative enzymes. Chemical approaches to date have not replicated such exquisite mediation. Oxidoreductases efficiently promote folding by the cooperative effects of oxidative reactivity for disulfide-bond formation in the client unfolded protein and chaperone activity to mitigate aggregation. Conventional synthetic folding promotors mimic the redox-reactivity of thiol/disulfide units but do not address client-recognition units for inhibiting aggregation. Herein, we report thiol/disulfide compounds containing client-recognition units, which act as synthetic oxidoreductase-mimics. For example, compound βCDWSH/SS bears a thiol/disulfide unit at the wide rim of β-cyclodextrin as a client recognition unit. βCDWSH/SS shows promiscuous binding to client proteins, mitigates protein aggregation, and accelerates disulfide-bond formation. In contrast, positioning a thiol/disulfide unit at the narrow rim of β-cyclodextrin promotes folding less effectively through preferential interactions at specific residues, resulting in aggregation. The combination of promiscuous client-binding and redox reactivity is effective for the design of synthetic folding promoters. βCDWSH/SS accelerates oxidative protein folding at highly condensed sub-millimolar protein concentrations. |
| 書誌情報 |
en : Chemical Science
巻 15,
号 32,
p. 12676,
発行日 2024-07-29
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| 収録物ID |
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収録物識別子タイプ |
EISSN |
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収録物識別子 |
20416539 |
| 出版者 |
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出版者 |
The Royal Society of Chemistry |
| 権利情報 |
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権利情報Resource |
https://creativecommons.org/licenses/by-nc/3.0/ |
|
権利情報 |
Creative Commons Attribution-NonCommercial 3.0 Unported |
| EID |
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識別子 |
418583 |
| 言語 |
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言語 |
eng |
cs_15_32_12676.pdf (2.4 MB)
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