• 文献标题:   Polyoxometalate@magnetic graphene as versatile immobilization matrix of Ru(bpy)(3)(2+) for sensitive magneto-controlled electrochemiluminescence sensor and its application in biosensing
  • 文献类型:   Article
  • 作  者:   QIAN J, WANG K, JIN YC, YANG XW, JIANG L, YAN YT, DONG XY, LI HM, QIU BJ
  • 作者关键词:   magnetic graphene, polyoxometalate, ru bpy 3 2+, electrochemiluminescence, nadh, llactate
  • 出版物名称:   BIOSENSORS BIOELECTRONICS
  • ISSN:   0956-5663 EI 1873-4235
  • 通讯作者地址:   Jiangsu Univ
  • 被引频次:   22
  • DOI:   10.1016/j.bios.2014.02.005
  • 出版年:   2014

▎ 摘  要

We demonstrated here the exploration of polyoxometalate (POM) coated magnetic Fe3O4/reduced graphene oxide (POM@mrGO) composite as the versatile immobilization matrix for the electrochemiluminescence (ECL) agent Ru(bpy)(3)(2+). The effective modification of Ru(bpy)(3)(2+)/POM@mrGO hybrid simply involved using magnetic electrode showed 10-fold ECL intensity increase than that observed for Ru(bpy)(3)(2+)/Nafion@mrGO to the same concentration of nicotinamide adenine dinucleotide (NADH), which is largely due to POM's good electrocatalytic activity towards NADH oxidation. These findings allowed the stable and ultrasensitive ECL detection of NADH as low as 0.1 nM. The good stability and high sensitivity of the magneto-controlled ECL sensor enabled us to explore the feasibility of applying the sensing platform to fabricating the ECL biosensors in which the NADH was produced from the dehydrogenase-based enzymatic reaction in the presence of NAD(+) cofactor. With L-lactate dehydrogenase as a model, a (L)-Iactate biosensor was successfully constructed where we showed that the ECL intensity of the biosensor increased with the increasing L-lactate concentration. Excellent performance of the presented biosensor has been achieved including a wide linear range extended from 5.0 x 10(-9) M to 5.0 x 10(-4) M and an extremely low detection limit of 0.4 nM. Such sensing strategy combines enzymatic selectivity with simple sensor preparation can be used as a new and biocompatible platform for dehydrogenase-based ECL biosensing. (c) 2014 Elsevier B.V. All rights reserved.