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Horseradish Peroxidase-Driven fluorescent Labeling of Nanotubes with Quantum Dots
Author(s) -
Vladimir V. Didenko,
David S. Baskin
Publication year - 2006
Publication title -
biotechniques
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.617
H-Index - 131
eISSN - 1940-9818
pISSN - 0736-6205
DOI - 10.2144/000112110
Subject(s) - biotinylation , horseradish peroxidase , fluorescence , carbon nanotube , streptavidin , quantum dot , chemistry , conjugated system , peroxidase , biotin , nanotechnology , biophysics , materials science , enzyme , biochemistry , organic chemistry , biology , polymer , physics , quantum mechanics
We describe the first enzyme-driven technique for fluorescent labeling of single-walled carbon nanotubes (SWNTs). The labeling was performed via enzymatic biotinylation of nanotubes in the tyramide-horseradish peroxidase (HRP) reaction. Both direct and indirect fuorescent labeling of SWNTs was achieved using either biotinyl tyramide or fluorescently tagged tyramides. Biotinylated SWNTs later reacted with streptavidin-conjugated fluorophores. Linking semiconductor nanocrystals, quantum dots (Q-dots), to the surface of nanotubes resulted in their fluorescent visualization, whereas conventional fluorophores bound to SWNTs directly or through biotin-streptavidin linkage, were completely quenched. Enzymatic biotinylation permits fluorescent visualization of carbon nanotubes, which could be useful for a number of biomedical applications. In addition, other organic molecules such as proteins, antibodies, or DNA can be conjugated to biotinylated SWNTs using this approach.

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