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

Jorge Hernando; Tahmineh Pourrostami; Jose A. Garrido; Oliver A. Williams; Dieter M. Gruen; Alexander Kromka; Doris Steinmüller; Martin Stutzmann

doi:10.1016/j.diamond.2006.04.005

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

Jorge Hernando
, Tahmineh Pourrostami
, Jose A. Garrido
, Oliver A. Williams
, Dieter M. Gruen
, Alexander Kromka
, Doris Steinmüller
, Martin Stutzmann

TUM Emeriti of Excellence

Research output: Contribution to journal › Article › peer-review

55 Scopus citations

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.

Original language	English
Pages (from-to)	138-143
Number of pages	6
Journal	Diamond and Related Materials
Volume	16
Issue number	1
DOIs	https://doi.org/10.1016/j.diamond.2006.04.005
State	Published - Jan 2007

Keywords

Biomaterials
Diamond film
Electrochemical
Nanocrystalline

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10.1016/j.diamond.2006.04.005

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title = "Immobilization of horseradish peroxidase via an amino silane on oxidized ultrananocrystalline diamond",

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.",

keywords = "Biomaterials, Diamond film, Electrochemical, Nanocrystalline",

author = "Jorge Hernando and Tahmineh Pourrostami and Garrido, \{Jose A.\} and Williams, \{Oliver A.\} and Gruen, \{Dieter M.\} and Alexander Kromka and Doris Steinm{\"u}ller and Martin Stutzmann",

year = "2007",

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doi = "10.1016/j.diamond.2006.04.005",

language = "English",

volume = "16",

pages = "138--143",

journal = "Diamond and Related Materials",

issn = "0925-9635",

publisher = "Elsevier B.V.",

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TY - JOUR

T1 - Immobilization of horseradish peroxidase via an amino silane on oxidized ultrananocrystalline diamond

AU - Hernando, Jorge

AU - Pourrostami, Tahmineh

AU - Garrido, Jose A.

AU - Williams, Oliver A.

AU - Gruen, Dieter M.

AU - Kromka, Alexander

AU - Steinmüller, Doris

AU - Stutzmann, Martin

PY - 2007/1

Y1 - 2007/1

N2 - 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.

AB - 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.

KW - Biomaterials

KW - Diamond film

KW - Electrochemical

KW - Nanocrystalline

UR - https://www.scopus.com/pages/publications/33751328553

U2 - 10.1016/j.diamond.2006.04.005

DO - 10.1016/j.diamond.2006.04.005

M3 - Article

AN - SCOPUS:33751328553

SN - 0925-9635

VL - 16

SP - 138

EP - 143

JO - Diamond and Related Materials

JF - Diamond and Related Materials

IS - 1

ER -

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

Abstract

Keywords

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