期刊
ANALYTICAL CHEMISTRY
卷 91, 期 12, 页码 7828-7834出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.9b01553
关键词
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资金
- National Key Research and Development Program of China [2016YFA0201301]
- National Natural Science Foundation of China [21435005, 21627808, 21605139]
- Key Research Program of Frontier Sciences, CAS [QYZDY-SSW-SLH019]
- Youth Innovation Promotion Association, CAS [2018258]
- Open Project of State Key Laboratory of Supramolecular Structure and Materials [sldssm2019023]
Alkaline phosphatase (ALP) usually acts as a signal transmitter in enzyme-linked immunosorbent assay (ELBA); therefore, developing an attractive ALP activity assay, especially using a preferable substrate, would help improve the efficiency and convenience of ELISA in practical applications. Herein we have first prepared an original and creative substrate, named m-hydroxyphenyl phosphate sodium salt (m-HPP), with a desirable dephosphorylation site for ALP. On the basis of the ALP-catalyzed hydrolysis of m-HPP to resorcinol and its subsequent specific nucleophilic reaction with dopamine, we have exploited a fluorometric and colorimetric dual-readout ALP activity assay and ALP-based ELISA system. Under the employed experimental conditions, highly sensitive and specific assay of ALP and cardiac troponin I (cTnI) has been accomplished in a straightforward way. Furthermore, the commendable sensing performance of our proposed ELISA in the determination of the cTnI level in diluted human serum unambiguously illustrates great potential in the early' diagnosis of acute myocardial infarction.
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