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. 2014:2014:705068.
doi: 10.1155/2014/705068. Epub 2014 May 22.

Characterization of modified magnetite nanoparticles for albumin immobilization

Affiliations

Characterization of modified magnetite nanoparticles for albumin immobilization

A K Bordbar et al. Biotechnol Res Int. 2014.

Abstract

Magnetite Fe3O4 nanoparticles (NPs) were prepared by chemical coprecipitation method. Silica-coated magnetite NPs were prepared by sol-gel reaction, subsequently coated with 3-aminopropyltriethoxysilane (APTES) via silanization reaction, and then were activated with 2,4,6-trichloro-1,3,5-triazine (TCT) and covalently immobilized with bovine serum albumin (BSA). The size and structure of the particles were characterized by transmission electron microscopy (TEM), X-ray powder diffraction (XRD), and dynamic light scattering (DLS) techniques. The immobilization was confirmed by Fourier transform infrared spectroscopy (FT-IR). XRD analysis showed that the binding process has not done any phase change to Fe3O4. The immobilization time for this process was 4 h and the amount of immobilized BSA for the initial value of 1.05 mg BSA was about 120 mg/gr nanoparticles. Also, the influences of three different buffer solutions and ionic strength on covalent immobilization were evaluated.

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Figures

Scheme 1
Scheme 1
Covalent attachment of BSA on modified magnetite nanoparticles.
Figure 1
Figure 1
The DLS (a) and TEM (b) of silica-coated MNPs.
Figure 2
Figure 2
FT-IR spectra of the naked Fe3O4, APTES-modified, and TCT-APTES-modified magnetite nanoparticles.
Figure 3
Figure 3
FT-IR spectra of the modified magnetite nanoparticles with (top) and without (bottom) bound BSA.
Figure 4
Figure 4
XRD patterns for magnetic nanoparticles with (a) and without (b) BSA.
Figure 5
Figure 5
Effect of reaction time on the amount of immobilized BSA.
Figure 6
Figure 6
Effect of the initial amount of protein on the amount of immobilized BSA.
Figure 7
Figure 7
Effect of the ionic strength on the immobilization percentage.

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