Dynamic frustrated charge hotspots created by charge density modulation sequester globular proteins into complex coacervates
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- K C, Biplab
- 九州大学大学院システム生命科学府システム生命科学専攻
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- 新居, 輝樹
- 九州大学大学院工学研究院応用化学部門
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- 森, 健
- 九州大学大学院工学研究院応用化学部門 九州大学未来化学創造センター
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- 片山, 佳樹
- 九州大学大学院工学研究院応用化学部門 九州大学未来化学創造センター 九州大学分子システム科学センター
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- 岸村, 顕広
- 九州大学大学院工学研究院応用化学部門 九州大学未来化学創造センター 九州大学分子システム科学センター
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説明
This study presents a simple strategy for the sequestration of globular proteins as clients into synthetic polypeptide-based complex coacervates as a scaffold, thereby recapitulating the scaffold-client interaction found in biological condensates. Considering the low net charges of scaffold proteins participating in biological condensates, the linear charge density (σ) on the polyanion, polyethylene glycol-b-poly(aspartic acids), was reduced by introducing hydroxypropyl or butyl moieties as a charge-neutral pendant group. Complex coacervate prepared from the series of reduced-σ polyanions and the polycation, homo-poly-L-lysine, could act as a scaffold that sequestered various globular proteins with high encapsulation efficiency (>80%), which sometimes involved further agglomerations in the coacervates. The sequestration of proteins was basically driven by electrostatic interaction, and therefore depended on the ionic strength and charges of the proteins. However, based on the results of polymer partitioning in the coacervate in the presence or absence of proteins, charge ratios between cationic and anionic polymers were maintained at the charge ratio of unity. Therefore, the origin of the electrostatic interaction with proteins is considered to be dynamic frustrated charges in the complex coacervates created by non-neutralized charges on polymer chains. Furthermore, fluorescence recovery after photobleaching (FRAP) measurements showed that the interaction of side-chains and proteins changed the dynamic property of coacervates. It also suggested that the physical properties of the condensate are tunable before and after the sequestration of globular proteins. The present rational design approach of the scaffold-client interaction is helpful for basic life-science research and the applied frontier of artificial organelles.
収録刊行物
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- Chemical Science
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Chemical Science 14 (24), 6608-6620, 2023-05-19
Royal Society of Chemistry (RSC)
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詳細情報 詳細情報について
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- CRID
- 1050018428980201216
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- NII書誌ID
- AA12555653
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- ISSN
- 20416539
- 20416520
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- HANDLE
- 2324/7173543
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB