| Description |
Author Affiliation: Tan H ( Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Key Laboratory of Chemical Biology, Jiangxi Province, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, PR China. Electronic address: hltan@jxnu.edu.cn.); Li Q ( Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Key Laboratory of Chemical Biology, Jiangxi Province, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, PR China.); Zhou Z ( Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Key Laboratory of Chemical Biology, Jiangxi Province, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, PR China.); Ma C ( Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Key Laboratory of Chemical Biology, Jiangxi Province, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, PR China.); Song Y ( Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Key Laboratory of Chemical Biology, Jiangxi Province, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, PR China.); Xu F ( Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Key Laboratory of Chemical Biology, Jiangxi Province, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, PR China.); Wang L ( Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Key Laboratory of Chemical Biology, Jiangxi Province, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, PR China. Electronic address: lwanggroup@aliyun.com.) |
| Abstract |
Metal-organic frameworks (MOFs) with tunable structures and properties have recently been emerged as very interesting functional materials. However, the catalytic properties of MOFs as enzymatic mimics remain to be further investigated. In this work, we for the first time demonstrated the peroxidase-like activity of copper-based MOFs (HKUST-1) by employing thiamine (TH) as a peroxidase substrate. In the presence of H2O2, HKUST-1 can catalyze efficiently the conversion of non-fluorescent TH to strong fluorescent thiochrome. The catalytic activity of HKUST-1 is highly dependent on the temperature, pH and H2O2 concentrations. As a peroxidase mimic, HKUST-1 not only has the features of low cost, high stability and easy preparation, but also follows Michaelis-Menten behaviors and shows stronger affinity to TH than horseradish peroxidase (HRP). Based on the peroxidase-like activity of HKUST-1, a simple and sensitive fluorescent method for TH detection has been developed. As low as 1 µM TH can be detected with a linear range from 4 to 700 µM. The detection limit for TH is about 50 fold lower than that of HRP-based fluorescent assay. The proposed method was successfully applied to detect TH in tablets and urine samples and showed a satisfactory result. We believed that the present work could improve the understanding of catalytic behaviors of MOFs as enzymatic mimics and find out a wider application in bioanalysis. |
