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Immobilization of horseradish peroxidase via an amino silane on oxidized ultrananocrystalline diamond

Hernando, J., Pourrostami, T., Garrido, J. A., Williams, Oliver Aneurin, Gruen, D. M., Kromka, A., Steinmuller, D. and Stutzmann, M. 2007. Immobilization of horseradish peroxidase via an amino silane on oxidized ultrananocrystalline diamond. Diamond and Related Materials 16 (1) , pp. 138-143. 10.1016/j.diamond.2006.04.005

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Abstract

We discuss the complete functionalization of nitrogen-doped ultrananocrystalline diamond (UNCD) films, starting from an oxidized surface. First, the presence of hydroxyl groups on oxidized nanocrystalline diamond (NCD) was confirmed by fluorescence microscopy. Next, the grafting of a linker molecule such as 3-aminopropylmethyldiethoxysilane on oxidized NCD was confirmed by fluorescence microscopy and X-ray photoelectron spectroscopy (XPS). Then the horseradish peroxidase (HRP) enzyme was immobilized on silane-modified initially oxidized UNCD. The HRP-modified UNCD was characterized by electrochemical techniques, such as faradaic cyclic voltammetry and the amperometric response to H2O2. This response to H2O2 is discussed in terms of the layer-by-layer configuration used and the electronic properties of conducting UNCD.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Physics and Astronomy
Subjects: Q Science > QC Physics
Uncontrolled Keywords: Diamond film; Nanocrystalline; Electrochemical; Biomaterials
Publisher: Elsevier
ISSN: 0925-9635
Last Modified: 04 Jun 2017 04:11
URI: http://orca.cf.ac.uk/id/eprint/34158

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