Fabrication of a silica coating on magnetic γ-Fe2O 3 nanoparticles by an immobilized enzyme

Mohammed Ibrahim Shukoor; Filipe Natalio; Helen Annal Therese; Muhammad Nawaz Tahir; Vadim Ksenofontov; Martin Panthöfer; Marc Eberhardt; Patrick Theato; Heinz Christoph Schröder; Werner E.G. Müller; Wolfgang Tremel

doi:10.1021/cm7029954

Fabrication of a silica coating on magnetic γ-Fe₂O ₃ nanoparticles by an immobilized enzyme

Mohammed Ibrahim Shukoor
, Filipe Natalio
, Helen Annal Therese
, Muhammad Nawaz Tahir
, Vadim Ksenofontov
, Martin Panthöfer
, Marc Eberhardt
, Patrick Theato
, Heinz Christoph Schröder
, Werner E.G. Müller
, Wolfgang Tremel^*

^*Corresponding author for this work

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

67 Scopus citations

Abstract

Silicatein, a hydrolytic protein encountered in marine sponges, was immobilized on maghemite (γ-Fe₂O₃) nanoparticles that were surface functionalized with a reactive mulfunctional polymer. This polymer carries an anchor group based on dopamine which is capable of binding to the γ-Fe₂O₃ surface and a reactive functional group which allows binding of various biomolecules onto inorganic nanoparticles. This functional nitrilotriacetic acid (NTA) group allows immobilization of His-tagged silicatein on the surface of the γ-Fe₂Os nanoparticles. The surface-bound protein retains its native hydrolytic activity to catalyze formation of silica through copolymerization of alkoxysilanes Si(OR)₄. Functionalization of the magnetic nanoparticles and the architecture of the SiO₂-coated γ-Fe₂O₃ nanoparticles was confirmed by TEM studies as well as by FT-IR and optical microscopy.

Original language	English
Pages (from-to)	3567-3573
Number of pages	7
Journal	Chemistry of Materials
Volume	20
Issue number	11
DOIs	https://doi.org/10.1021/cm7029954
State	Published - 10 Jun 2008
Externally published	Yes

ASJC Scopus subject areas

General Chemistry
General Chemical Engineering
Materials Chemistry

Access to Document

10.1021/cm7029954

Cite this

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title = "Fabrication of a silica coating on magnetic γ-Fe2O 3 nanoparticles by an immobilized enzyme",

abstract = "Silicatein, a hydrolytic protein encountered in marine sponges, was immobilized on maghemite (γ-Fe2O3) nanoparticles that were surface functionalized with a reactive mulfunctional polymer. This polymer carries an anchor group based on dopamine which is capable of binding to the γ-Fe2O3 surface and a reactive functional group which allows binding of various biomolecules onto inorganic nanoparticles. This functional nitrilotriacetic acid (NTA) group allows immobilization of His-tagged silicatein on the surface of the γ-Fe2Os nanoparticles. The surface-bound protein retains its native hydrolytic activity to catalyze formation of silica through copolymerization of alkoxysilanes Si(OR)4. Functionalization of the magnetic nanoparticles and the architecture of the SiO2-coated γ-Fe2O3 nanoparticles was confirmed by TEM studies as well as by FT-IR and optical microscopy.",

author = "Shukoor, \{Mohammed Ibrahim\} and Filipe Natalio and Therese, \{Helen Annal\} and Tahir, \{Muhammad Nawaz\} and Vadim Ksenofontov and Martin Panth{\"o}fer and Marc Eberhardt and Patrick Theato and Schr{\"o}der, \{Heinz Christoph\} and M{\"u}ller, \{Werner E.G.\} and Wolfgang Tremel",

year = "2008",

month = jun,

day = "10",

doi = "10.1021/cm7029954",

language = "English",

volume = "20",

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journal = "Chemistry of Materials",

issn = "0897-4756",

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TY - JOUR

T1 - Fabrication of a silica coating on magnetic γ-Fe2O 3 nanoparticles by an immobilized enzyme

AU - Shukoor, Mohammed Ibrahim

AU - Natalio, Filipe

AU - Therese, Helen Annal

AU - Tahir, Muhammad Nawaz

AU - Ksenofontov, Vadim

AU - Panthöfer, Martin

AU - Eberhardt, Marc

AU - Theato, Patrick

AU - Schröder, Heinz Christoph

AU - Müller, Werner E.G.

AU - Tremel, Wolfgang

PY - 2008/6/10

Y1 - 2008/6/10

N2 - Silicatein, a hydrolytic protein encountered in marine sponges, was immobilized on maghemite (γ-Fe2O3) nanoparticles that were surface functionalized with a reactive mulfunctional polymer. This polymer carries an anchor group based on dopamine which is capable of binding to the γ-Fe2O3 surface and a reactive functional group which allows binding of various biomolecules onto inorganic nanoparticles. This functional nitrilotriacetic acid (NTA) group allows immobilization of His-tagged silicatein on the surface of the γ-Fe2Os nanoparticles. The surface-bound protein retains its native hydrolytic activity to catalyze formation of silica through copolymerization of alkoxysilanes Si(OR)4. Functionalization of the magnetic nanoparticles and the architecture of the SiO2-coated γ-Fe2O3 nanoparticles was confirmed by TEM studies as well as by FT-IR and optical microscopy.

AB - Silicatein, a hydrolytic protein encountered in marine sponges, was immobilized on maghemite (γ-Fe2O3) nanoparticles that were surface functionalized with a reactive mulfunctional polymer. This polymer carries an anchor group based on dopamine which is capable of binding to the γ-Fe2O3 surface and a reactive functional group which allows binding of various biomolecules onto inorganic nanoparticles. This functional nitrilotriacetic acid (NTA) group allows immobilization of His-tagged silicatein on the surface of the γ-Fe2Os nanoparticles. The surface-bound protein retains its native hydrolytic activity to catalyze formation of silica through copolymerization of alkoxysilanes Si(OR)4. Functionalization of the magnetic nanoparticles and the architecture of the SiO2-coated γ-Fe2O3 nanoparticles was confirmed by TEM studies as well as by FT-IR and optical microscopy.

UR - https://www.scopus.com/pages/publications/47049099620

U2 - 10.1021/cm7029954

DO - 10.1021/cm7029954

M3 - Article

AN - SCOPUS:47049099620

SN - 0897-4756

VL - 20

SP - 3567

EP - 3573

JO - Chemistry of Materials

JF - Chemistry of Materials

IS - 11