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Supramolecular Construction of Biohybrid Nanozymes Based on the Molecular Chaperone GroEL as a Promiscuous Scaffold
ACS Biomaterials Science & Engineering ( IF 5.4 ) Pub Date : 2020-01-15 , DOI: 10.1021/acsbiomaterials.9b00997 Xiaoqiang Wang 1 , Shixin Li 1 , Chao Wang 1 , Christopher J. Mujuni 1 , Tongtao Yue 1 , Fang Huang 1
ACS Biomaterials Science & Engineering ( IF 5.4 ) Pub Date : 2020-01-15 , DOI: 10.1021/acsbiomaterials.9b00997 Xiaoqiang Wang 1 , Shixin Li 1 , Chao Wang 1 , Christopher J. Mujuni 1 , Tongtao Yue 1 , Fang Huang 1
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The study of enzymatic reactions in a confined space can provide valuable insight into the natural selection of nanocompartments for biocatalytic processes. Design of nanozyme capsules with the barrel-shaped protein cage of GroEL has been proposed as a promising means to constrain chemical reactions in a spatiotemporally controllable manner. Herein, we further demonstrate with hemin that the open GroEL cavity can provide a favorable microenvironment for shielding hydrophobic catalytically active species. Meanwhile, it is shown that the GroEL-caged hemin nanozyme not only has a significantly higher catalytic activity than merely dispersed hemin but also exhibits substrate specificity in the model oxidation reactions, which is a merit lacking in natural hemoproteins. To understand the underlying mechanism behind this supramolecular assembly, molecular docking and molecular dynamics simulations were performed to study the detailed interactions of hemin with the protein cage. This revealed the most likely binding mode and preferred binding residues in the paired hydrophobic α-helices lining the GroEL cavity which are genetically encoded for substrate capture. Finally, we demonstrate that the hemin-GroEL nanozyme has great potential in label-free fluorometric molecular detection when combined with suitable substrates such as homovanillic acid. We believe that our strategy is an advantageous tool for studying confined biocatalytic kinetics as simple mimics of protein-based organelles found in nature and for designing diverse nanozymes or bio-nanoreactors with the promiscuous GroEL binding cavity.
中文翻译：
基于分子伴侣GroEL作为混杂支架的生物杂交纳米酶的超分子构建。
在密闭空间中进行酶促反应的研究可以为自然选择用于生物催化过程的纳米隔室提供有价值的见解。已经提出了设计具有GroEL桶形蛋白笼的纳米酶胶囊的方法，该方法有望以时空可控的方式限制化学反应。在这里，我们用血红素进一步证明，开放的GroEL腔可以提供有利的微环境来屏蔽疏水的催化活性物质。同时，表明GroEL-笼罩的血红素纳米酶不仅具有比仅分散的血红素显着更高的催化活性，而且在模型氧化反应中表现出底物特异性，这是天然血蛋白缺乏的优点。要了解这种超分子组装背后的潜在机制，进行分子对接和分子动力学模拟以研究血红素与蛋白笼的详细相互作用。这揭示了在GroEL腔内衬的成对疏水性α-螺旋中最有可能的结合模式和优选的结合残基，这些残基通过基因编码用于底物捕获。最后，我们证明当与合适的底物（如高香草酸）结合使用时，hemin-GroEL纳米酶在无标记荧光分子检测中具有巨大潜力。我们认为，我们的策略是研究局限性生物催化动力学的一种有利工具，该动力学是自然界中基于蛋白质的细胞器的简单模拟，并且可以用于设计具有混杂GroEL结合腔的多种纳米酶或生物纳米反应器。
更新日期：2020-01-15
中文翻译：
基于分子伴侣GroEL作为混杂支架的生物杂交纳米酶的超分子构建。
在密闭空间中进行酶促反应的研究可以为自然选择用于生物催化过程的纳米隔室提供有价值的见解。已经提出了设计具有GroEL桶形蛋白笼的纳米酶胶囊的方法，该方法有望以时空可控的方式限制化学反应。在这里，我们用血红素进一步证明，开放的GroEL腔可以提供有利的微环境来屏蔽疏水的催化活性物质。同时，表明GroEL-笼罩的血红素纳米酶不仅具有比仅分散的血红素显着更高的催化活性，而且在模型氧化反应中表现出底物特异性，这是天然血蛋白缺乏的优点。要了解这种超分子组装背后的潜在机制，进行分子对接和分子动力学模拟以研究血红素与蛋白笼的详细相互作用。这揭示了在GroEL腔内衬的成对疏水性α-螺旋中最有可能的结合模式和优选的结合残基，这些残基通过基因编码用于底物捕获。最后，我们证明当与合适的底物（如高香草酸）结合使用时，hemin-GroEL纳米酶在无标记荧光分子检测中具有巨大潜力。我们认为，我们的策略是研究局限性生物催化动力学的一种有利工具，该动力学是自然界中基于蛋白质的细胞器的简单模拟，并且可以用于设计具有混杂GroEL结合腔的多种纳米酶或生物纳米反应器。
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