Characterization of an interaction between functionalized carbon nanotubes and an enzyme

Marc In Het Panhuis, Carolina Salvador-Morales, Edward Franklin, Gordon Chambers, Antonio Fonseca, Janos B. Nagy, Werner J. Blau, Andrew I. Minett

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Carbon nanotubes (CNTs) did not exhibit strong interactions with Biliverdin IXB 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.

    Original languageEnglish
    Pages (from-to)209-213
    Number of pages5
    JournalJournal of Nanoscience and Nanotechnology
    Volume3
    Issue number3
    DOIs
    Publication statusPublished - Jun 2003

    Keywords

    • Carbon nanotubes
    • Enzymes
    • Functionalization
    • Raman
    • Sensing

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