Protein-Metal Organic Framework Hybrid Composites with Intrinsic Peroxidase-like Activity as a Colorimetric Biosensing Platform
Protein-Metal Organic Framework Hybrid Composites with Intrinsic Peroxidase-like Activity as a Colorimetric Biosensing Platform
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具有内在过氧化物酶样活性的蛋白质-金属有机框架杂化复合材料作为比色生物传感平台。
DOI：
10.1021/acsami.6b09893
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发表时间：
2016-10-26
影响因子：
9.5
通讯作者：
Yang, Huanghao
中科院分区：
文献类型：
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作者：
Yin, Yuqing;Gao, Chenling;Yang, Huanghao
人工酶模拟物受到了相当大的关注，因为天然酶具有一些显着的缺点，包括酶自溶、催化活性低、回收率差以及对环境变化的稳定性低。本文以牛血红蛋白（BHb）和咪唑骨架-8（ZIF-8）为模型反应体系，采用一锅法合成了血红素蛋白-金属有机骨架杂化复合材料（H-MOFs）。令人惊讶的是，新的混合复合材料表现出423%的增加过氧化物酶样催化活性相比，游离BHb。利用H-MOFs独特的孔结构和高催化性能，构建了基于H-MOFs的比色生物传感平台，并将其应用于H2 O2和苯酚的快速、灵敏检测。通过肉眼观察，每种分析物的相应检测限低至1.0 μM，线性范围宽（H2 O2为0-800 μM，苯酚为0-200 μM）。利用该平台实现了细胞中痕量H2 O2和污水中苯酚的可视化检测。还检查了H-MOFs的稳定性，并且观察到优异的再现性和可回收性而不损失其活性。此外，H-MOFs的一般适用性也进行了研究，通过使用其他血红素蛋白（辣根过氧化物酶，肌红蛋白），相应的催化活性分别提高了291%和273%。本工作不仅拓展了MOFs的应用范围，而且为生物和环境样品的分析提供了一种新的技术。
Artificial enzyme mimetics have received considerable attention because natural enzymes have some significant drawbacks, including enzyme autolysis, low catalytic activity, poor recovery, and low stability to environmental changes. Herein, we demonstrated a facile approach for one-pot synthesis of hemeprotein-metal organic framework hybrid composites (H-MOFs) by using bovine hemoglobin (BHb) and zeolitic imidazolate framework-8 (ZIF-8) as a model reaction system. Surprisingly, the new hybrid composites exhibit 423% increase in peroxidase-like catalytic activity compared to free BHb. Taking advantages of the unique pore structure of H-MOFs with high catalytic property, a H-MOFs-based colorimetric biosensing platform was newly constructed and applied for the fast and sensitive detection of hydrogen peroxide (H2O2) and phenol. The corresponding detection limits as low as 1.0 μM for each analyte with wide linear ranges (0-800 μM for H2O2 and 0-200 μM for phenol) were obtained by naked-eye visualization. Significantly, a sensitive and selective method for visual assay of trace H2O2 in cells and phenol in sewage was achieved with this platform. The stability of H-MOFs was also examined, and excellent reproducibility and recyclability without losing in their activity were observed. In addition, the general applicability of H-MOFs was also investigated by using other hemeproteins (horseradish peroxidase, and myoglobin), and the corresponding catalytic activities were 291% and 273% enhancement, respectively. This present work not only expands the application of MOFs but also provides an alternative technique for biological and environmental sample assay.