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

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54 Zitate (Scopus)

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.

Originalsprache	Englisch
Seiten (von - bis)	138-143
Seitenumfang	6
Fachzeitschrift	Diamond and Related Materials
Jahrgang	16
Ausgabenummer	1
DOIs	https://doi.org/10.1016/j.diamond.2006.04.005
Publikationsstatus	Veröffentlicht - Jan. 2007

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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",

month = jan,

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

language = "English",

volume = "16",

pages = "138--143",

journal = "Diamond and Related Materials",

issn = "0925-9635",

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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 - http://www.scopus.com/inward/record.url?scp=33751328553&partnerID=8YFLogxK

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

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