Nano-hard template synthesis of pure mesoporous NiO and its application for streptavidin protein immobilization

Wahab, Mohammad A. and Darain, Farzana (2014) Nano-hard template synthesis of pure mesoporous NiO and its application for streptavidin protein immobilization. Nanotechnology, 25 16: 1-7. doi:10.1088/0957-4484/25/16/165701


Author Wahab, Mohammad A.
Darain, Farzana
Title Nano-hard template synthesis of pure mesoporous NiO and its application for streptavidin protein immobilization
Journal name Nanotechnology   Check publisher's open access policy
ISSN 1361-6528
0957-4484
Publication date 2014-04-25
Year available 2014
Sub-type Article (original research)
DOI 10.1088/0957-4484/25/16/165701
Open Access Status Not Open Access
Volume 25
Issue 16
Start page 1
End page 7
Total pages 7
Place of publication Bristol, United Kingdom
Publisher Institute of Physics Publishing
Language eng
Formatted abstract
A simple and efficient immobilization of streptavidin protein (with hexa-histidine tag) onto the surface of mesoporous NiO is described. Before immobilization of streptavidin protein (with hexa-histidine tag) onto the surface of mesoporous NiO, we first synthesized well-organized mesoporous NiO by a nanocasting method using mesoporous silica SBA-15 as the hard template. Then, the well-organized mesoporous NiO particles were characterized by small angle x-ray diffraction (XRD), wide angle XRD, nitrogen adsorption/desorption, and transmission electron microscopy (TEM). TEM and small angle XRD suggested the formation of mesoporous NiO materials, whereas the wide angle XRD pattern of mesoporous NiO indicated that the nickel precursor had been transformed into crystalline NiO. The N2 sorption experiments demonstrated that the mesoporous NiO particles had a high surface area of 281 m2 g-1, a pore volume of 0.51 cm3 g-1 and a pore size of 4.8 nm. Next, the immobilization of streptavidin protein (with hexa-histidine tag) onto the surface of mesoporous NiO was studied. Detailed analysis using gel electrophoresis confirmed that this approach can efficiently bind his-tagged streptavidin onto the surface of mesoporous NiO material since the mesoporous NiO provides sufficient surface sites for the binding of streptavidin via non-covalent ligand binding with the histidine tag.
Keyword Mesoporous materials
Nanocasting hard templating approach
NiO
Streptavidin protein
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
Australian Institute for Bioengineering and Nanotechnology Publications
 
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