title: Characterization of an interaction between functionalized carbon nanotubes and an enzyme.
abstract: Carbon nanotubes (CNTs) did not exhibit strong interactions with Biliverdin IX beta reductase enzyme (BVRB) in water. With the use of noncovalent functionalization by the surfactant Triton X-100, the surfaces of the CNTs were changed from hydrophobic to hydrophilic. The hydrophilic surface of the CNT-Triton conjugate interacts with the hydrophilic surface of BVRB, thus creating a water-soluble complex. Results from ultracentrifugation through a sucrose gradient and gel electrophoresis show the presence of the enzyme. Raman spectroscopy confirmed that the enzyme indeed interacts with CNT-Triton conjugates.
mesh_terms: D000327:Adsorption; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D066298:In Vitro Techniques; D036103:Nanotechnology / Q000379:methods; D037742:Nanotubes, Carbon / Q000737:chemistry*; D017830:Octoxynol; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry*; D013059:Spectrum Analysis, Raman; D013501:Surface-Active Agents
chemical_list: D037742:Nanotubes, Carbon; D013501:Surface-Active Agents; D017830:Octoxynol; D044925:Oxidoreductases Acting on CH-CH Group Donors; C019789:biliverdin reductase