title: Supramolecular assembly of enzyme on functionalized graphene for electrochemical biosensing.
abstract: The self-assembly of cyclodextrin (CD) functionalized graphene (GR) and adamantane-modified horseradish peroxidase (HRP-ADA) by host-guest supramolecular interaction into novel nanostructures in aqueous solution is reported in the present study. Electrochemical impedance spectroscopy and cyclic voltammetry were applied to characterize the self-assembly process and study the electrochemical behaviors of the immobilized proteins. UV-vis spectra indicated that the native structure of HRP was maintained after the assembly, implying good biocompatibility of CD-functionalized GR (CD-GR). Furthermore, the HRP-ADA/CD-GR composites were utilized for the fabrication of enzyme electrodes (HRP-ADA/CD-GR electrodes). The proposed biosensor showed good reproducibility and high sensitivity to H2O2 with the detection limit of 0.1 μM. In the range of 0.7-35 μM, the catalytic reduction current of H2O2 was proportional to H2O2 concentration.
authors: College of Science, Jiangxi Agricultural University, Nanchang 330045, PR China.
authors: Li-Min
authors: LM
authors: Lu
authors: Xin-Lan
authors: XL
authors: Qiu
authors: Xiao-Bing
authors: XB
authors: Zhang
authors: Guo-Li
authors: GL
authors: Shen
authors: Weihong
authors: W
authors: Tan
authors: Ru-Qin
authors: RQ
authors: Yu
mesh_terms: D000218:Adamantane / Q000737:chemistry; D002384:Catalysis; D003505:Cyclodextrins / Q000737:chemistry; D058266:Dielectric Spectroscopy; D004563:Electrochemistry; D004800:Enzymes, Immobilized / Q000737:chemistry; D006108:Graphite / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000302:isolation & purification*; D049329:Nanostructures / Q000737:chemistry*
chemical_list: D003505:Cyclodextrins; D004800:Enzymes, Immobilized; D006108:Graphite; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D000218:Adamantane