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

Hernando, J., Pourrostami, T., Garrido, J. A., Williams, Oliver Aneurin ORCID: https://orcid.org/0000-0002-7210-3004, 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:	21 Oct 2022 08:42
URI:	https://orca.cardiff.ac.uk/id/eprint/34158

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