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Biomagnetic of Apatite-Coated Cobalt Ferrite: A Core – Shell Particle for Protein Adsorption and pH-Controlled Release

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ABSTRACT

Magnetic nanoparticle composite with a cobalt ferrite (CoFe2O4, (CF)) core and an apatite (Ap) coating was synthesized using a biomineralization process in which a modified simulated body fluid (1.5SBF) solution is the source of the calcium phosphate for the apatite formation. The core–shell structure formed after the citric acid–stabilized cobalt ferrite (CFCA) particles were incubated in the 1.5 SBF solution for 1 week. The mean particle size of CFCA-Ap is about 750 nm. A saturation magnetization of 15.56 emug-1 and a coercivity of 1808.5 Oe were observed for the CFCA-Ap obtained. Bovine serum albumin (BSA) was used as the model protein to study the adsorption and release of the proteins by the CFCA-Ap particles. The protein adsorption by the CFCA-Ap particles followed a more typical Freundlich than Langmuir adsorption isotherm. The BSA release as a function of time became less rapid as the CFCA-Ap particles were immersed in higher pH solution, thus indicating that the BSA release is dependent on the local pH.

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Adsorption curve of BSA loading onto the apatite (Ap)-coated citric acid–stabilized cobalt ferrite (CFCA) (CFCA-Ap) surface at pH = 7.4 and 37°C. The data points are expressed as mean ± SD; n = 3.
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Figure 7: Adsorption curve of BSA loading onto the apatite (Ap)-coated citric acid–stabilized cobalt ferrite (CFCA) (CFCA-Ap) surface at pH = 7.4 and 37°C. The data points are expressed as mean ± SD; n = 3.

Mentions: where qe is the BSA adsorption capacity for a unit amount of the particles (mg/g), C0 is the initial BSA concentration (mg/ml), Ce is the final or equilibrium BSA concentration (mg/ml), V is the volume of BSA solution (ml) (5 ml), and W is the weight of the particles added to the solution (mg). The results (Figure 7) show that the amount of bound BSA protein on the particles increases rapidly when the concentration of the BSA is in the range of 0.2–0.6 mg/ml and is lower when the concentration is above 0.6 mg/ml. The amount absorbed reaches a plateau at 1.0 mg/ml.


Biomagnetic of Apatite-Coated Cobalt Ferrite: A Core – Shell Particle for Protein Adsorption and pH-Controlled Release
Adsorption curve of BSA loading onto the apatite (Ap)-coated citric acid–stabilized cobalt ferrite (CFCA) (CFCA-Ap) surface at pH = 7.4 and 37°C. The data points are expressed as mean ± SD; n = 3.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3211243&req=5

Figure 7: Adsorption curve of BSA loading onto the apatite (Ap)-coated citric acid–stabilized cobalt ferrite (CFCA) (CFCA-Ap) surface at pH = 7.4 and 37°C. The data points are expressed as mean ± SD; n = 3.
Mentions: where qe is the BSA adsorption capacity for a unit amount of the particles (mg/g), C0 is the initial BSA concentration (mg/ml), Ce is the final or equilibrium BSA concentration (mg/ml), V is the volume of BSA solution (ml) (5 ml), and W is the weight of the particles added to the solution (mg). The results (Figure 7) show that the amount of bound BSA protein on the particles increases rapidly when the concentration of the BSA is in the range of 0.2–0.6 mg/ml and is lower when the concentration is above 0.6 mg/ml. The amount absorbed reaches a plateau at 1.0 mg/ml.

View Article: PubMed Central - HTML - PubMed

ABSTRACT

Magnetic nanoparticle composite with a cobalt ferrite (CoFe2O4, (CF)) core and an apatite (Ap) coating was synthesized using a biomineralization process in which a modified simulated body fluid (1.5SBF) solution is the source of the calcium phosphate for the apatite formation. The core–shell structure formed after the citric acid–stabilized cobalt ferrite (CFCA) particles were incubated in the 1.5 SBF solution for 1 week. The mean particle size of CFCA-Ap is about 750 nm. A saturation magnetization of 15.56 emug-1 and a coercivity of 1808.5 Oe were observed for the CFCA-Ap obtained. Bovine serum albumin (BSA) was used as the model protein to study the adsorption and release of the proteins by the CFCA-Ap particles. The protein adsorption by the CFCA-Ap particles followed a more typical Freundlich than Langmuir adsorption isotherm. The BSA release as a function of time became less rapid as the CFCA-Ap particles were immersed in higher pH solution, thus indicating that the BSA release is dependent on the local pH.

No MeSH data available.


Related in: MedlinePlus