文献类型：期刊文献

英文题名：In situ formation of fluorescent polydopamine catalyzed by peroxidase-mimicking FeCo-LDH for pyrophosphate ion and pyrophosphatase activity detection

作者：Xu, Xuechao[1,2];Zou, Xiaobo[1];Wu, Shuwen[1];Wang, Linjie[2];Niu, Xiangheng[2];Li, Xin[2];Pan, Jianming[2];Zhao, Hongli[3];Lan, Minbo[3]

机构：[1]Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China;[2]Jiangsu Univ, Sch Chem & Chem Engn, Inst Green Chem & Chem Technol, Zhenjiang 212013, Peoples R China;[3]East China Univ Sci & Technol, Sch Chem & Mol Engn, Shanghai Key Lab Funct Mat Chem, Shanghai 200237, Peoples R China

年份：2019

卷号：1053

起止页码：89

外文期刊名：ANALYTICA CHIMICA ACTA

收录：;EI(收录号：20185106268914);WOS:【SCI-EXPANDED(收录号:WOS:000457201600009)】；

基金：This work was supported by the National Natural Science Foundation of China (Nos. 21605061 and 31601549), the Natural Science Foundation of Jiangsu Province (Nos. BK20160489 and BK20160056), the Open Fund from the Shanghai Key Laboratory of Functional Materials Chemistry (No. SKLFMC201601), the Open Fund from the State Key Laboratory of Bioreactor Engineering, the Cultivation Project for Excellent Young Teachers in Jiangsu University, and the Postgraduate Research & Practice Innovation Program of Jiangsu Province (No. KYCX18_2275).

语种：英文

外文关键词：FeCo-LDH; Nanozyme; Fluorescent PDA; PPi; PPase

摘要：As pyrophosphate ion (PPi) and pyrophosphatase (PPase) play crucial roles in the pathological process of arthritis, determination of PPi and PPase in biological fluids turns to be of great importance for clinical diagnosis and therapy of arthritic diseases. In this work, we proposed a new fluorescent assay for PPi and PPase activity detection based on the competitive coordination chemistry of Fe3+ between PPi and an in situ formed fluorescent polydopamine (PDA). FeCo layered double hydroxide (FeCo-LDH) was explored as a peroxidase mimic to facilitate the in situ formation of fluorescent PDA from dopamine mediated by low-concentration H2O2 within 30 min; The formed fluorescent PDA could be significantly quenched by Fe3+ through forming a PDA-Fe3+ complex structure; When PPi existed, it coordinated Fe3+ competitively against PDA and inhibited the fluorescence quenching of PDA by Fe3+; When PPi was hydrolyzed under the catalysis of PPase, the Fe3+ ion could quench the fluorescence of the formed PDA again. With these principles, our fluorescent assay was able to detect PPi and PPase activity specifically, providing detection limits down to 54 mM and 0.13 U/L, respectively. Furthermore, accurate determination of PPi and PPase activity in spiked human serum was also demonstrated using the developed assay. (C) 2018 Elsevier B.V. All rights reserved.