title: Protein structure preservation by MWCNTs/RTIL nano-composite.
abstract: The structure changes of hemoglobin (Hb) and glucose oxidase (GOx), as two typical proteins, upon interaction with MWCNTs and MWCNTs-[BMIM]BF₄(-) was studied. The ability of MWCNTs and MWCNTs-([BMIM]BF₄(-)) for the achievement of direct electrochemistry of GOx and Hb and enhancing the electron transfer rate between proteins and electrode surface was compared. Also the data obtained by various techniques including UV-vis, fluorescence and circular dichroism spectroscopy revealed that the structure of Hb or GOx conjugated with supramolecular network of the nano-composite could be preserved much better than those absorbed on MWCNTs. It seems that ionic liquid provides a favorable microenvironment to maintain the protein native structures.
authors: Laboratory of Microanalysis, Institute of Biochemistry & Biophysics, University of Tehran, PO Box 13145-1384, Tehran, Iran.
authors: Somayeh
authors: S
authors: Karimi
authors: Hedayatollah
authors: H
authors: Ghourchian
authors: Aghdas
authors: A
authors: Banaei
mesh_terms: D001234:Aspergillus niger / Q000201:enzymology*; D002244:Carbon / Q000737:chemistry; D002942:Circular Dichroism; D004563:Electrochemistry; D004566:Electrodes; D005898:Glass / Q000737:chemistry; D005949:Glucose Oxidase / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D007093:Imidazoles / Q000737:chemistry; D052578:Ionic Liquids / Q000737:chemistry*; D053761:Nanocomposites / Q000737:chemistry*; D037742:Nanotubes, Carbon / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
chemical_list: C419324:1-butyl-3-methylimidazolium tetrafluoroborate; D006454:Hemoglobins; D007093:Imidazoles; D052578:Ionic Liquids; D037742:Nanotubes, Carbon; D002244:Carbon; D005949:Glucose Oxidase