Fe-Porphyrin-Based Covalent Organic Framework As a Novel Peroxidase Mimic for a One-Pot Glucose Colorimetric Assay

共价有机骨架 葡萄糖氧化酶 检出限 卟啉 显色的 共价键 辣根过氧化物酶 过氧化物酶 基质(水族馆) 纳米材料 化学 催化作用 过氧化氢 线性范围 组合化学 生物传感器 化学工程 材料科学 色谱法 纳米技术 有机化学 生物化学 工程类 海洋学 地质学
作者
Junning Wang,Xue Yang,Tianxiang Wei,Jianchun Bao,Qinshu Zhu,Zhihui Dai
出处
期刊:ACS applied bio materials [American Chemical Society]
卷期号:1 (2): 382-388 被引量:90
标识
DOI:10.1021/acsabm.8b00104
摘要

Covalent organic frameworks (COFs) have recently emerged as very fascinating porous polymers due to their attractive design synthesis and various applications. However, the catalytic application of COF materials as enzymatic mimics remains largely unexplored. In this work, the Fe-porphyrin-based covalent organic framework (Fe-COF) has been successfully synthesized through a facile postsynthetic strategy for the first time. In the presence of hydrogen peroxide (H2O2), the Fe-COF can catalyze a chromogenic substrate (3,3',5,5'-tetramethylbenzidine (TMB)) to produce color, and this just goes to show that it has an inner peroxidase-like activity. Moreover, the kinetic studies indicate that the Fe-COF nanomaterial has a higher affinity toward both the substrate H2O2 and TMB than the natural enzyme, horseradish peroxidase (HRP). Under the optimized conditions, the Fe-COF nanomaterial was applied in a colorimetric sensor for the sensitive detection of H2O2. The detection range was from 7 to 500 μM, and the detection limit was 1.1 μM. Furthermore, the combination of the Fe-COF with glucose oxidase (GOx) can be implemented to measure glucose by a one-pot method, and the obtained detection range was from 5 to 350 μM; the detection limit was 1.0 μM. It was proved that the sensor can be successfully used to detect the concentration of glucose in human serum samples. As a peroxidase mimic, the Fe-COF exhibits the advantages of easy preparation, good stability, and ultrahigh catalytic efficiency. We believed that the proposed method in this work would facilitate the applications of COF-based composites as enzymatic mimics in biomedical fields.
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