Electrochemical biosensing platform based on carboxymethyl cellulose functionalized reduced graphene oxide and hemoglobin hybrid nanocomposite film

Electrochemical biosensing platform based on carboxymethyl cellulose functionalized reduced graphene oxide and hemoglobin hybrid nanocomposite film
复制标题

基于羧甲基纤维素功能化还原氧化石墨烯和血红蛋白杂化纳米复合膜的电化学生物传感平台

DOI:
10.1016/j.snb.2013.03.007
复制
发表时间:
2013-06-01
影响因子:
8.4
通讯作者:
Fei, Junjie
Fei, Junjie
中科院分区:
化学1区
文献类型:
--
作者:
Cheng, Yao;Feng, Bo;Fei, Junjie

文献摘要

被引文献

相似文献

首次提出了一种基于羧甲基纤维素(CMC)功能化还原氧化石墨烯(rGO)纳米复合膜固定化血红蛋白(Hb)的新型生物相容性传感策略。采用扫描电镜(SEM)、x射线衍射(XRD)和电化学阻抗谱(EIS)对rGO-CMC/Hb膜进行了表征。采用循环伏安法研究了氧化石墨烯- cmc /Hb修饰电极的直接电化学性质。结果表明,Hb在修饰电极上保留了其生物活性,并表现出几个明确的准可逆氧化还原峰。固定化Hb对NO和H2O2的还原表现出良好的生物电催化活性。NO浓度在0.864 ~ 19.8亩M和19.8 ~ 48.6亩M范围内呈不同斜率的线性段。在3 σ时检出限为0.37 μ M。该传感器在0.083 ~ 13.94 μ M的宽线性范围内对H2O2具有良好的催化活性,在3 σ下的检出限为0.08 μ M。本文所采用的电化学方法简便易行,为蛋白质固定化和生物传感器的制备开辟了广阔的平台。(C) 2013 Elsevier B.V.版权所有
A novel, biocompatible sensing strategy based on carboxymethyl cellulose (CMC) functionalized reduced grapheme oxide (rGO) nanocomposite film for immobilizing the hemoglobin (Hb) was first developed. The rGO-CMC/Hb film was characterized by scanning electron microscopy (SEM), X-ray diffraction (XRD) and electrochemical impedance spectra (EIS). The direct electrochemistry of rGO-CMC/Hb modified electrodes were investigated by cyclic voltammetry. The results indicated that Hb retained its bioactivity on the modified electrode and showed a couple of well-defined and quasi-reversible redox peaks. The immobilized Hb exhibited excellent bioelectrocatalytic activity toward the reduction of NO and H2O2. Two linear segments with different slopes for NO concentration were from 0.864 mu M to 19.8 mu M and from 19.8 mu M to 48.6 mu M, respectively. The detection limit is 0.37 mu M at 3 sigma. The developed biosensor exhibited excellent catalytic activity toward H2O2 over a wide linear range of 0.083-13.94 mu M with a detection limit of 0.08 mu M at 3 sigma. The facile and easy electrochemical approach used in this paper may open up a promising platform for protein immobilization and biosensor preparation. (C) 2013 Elsevier B.V. All rights reserved.