Journal
BIOMATERIALS
Volume 30, Issue 27, Pages 4716-4722Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biomaterials.2009.05.005
Keywords
Superparamagnetic nanoparticle; Iron oxide; Peroxidase; Glucose detection
Funding
- NIH [CA114612, RNS066945]
- Hubei Natural Science Fund for Distinguished Young Scholars [2005ABB031]
- NIGMS [GM007767]
- American Foundation of Pharmaceutical Education (AFPE)
- NATIONAL CANCER INSTITUTE [R01CA114612] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007767] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS066945] Funding Source: NIH RePORTER
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Aside from their superparamagnetic properties exploited in clinical magnetic resonance imaging (MRI), it was recently discovered that magnetic, iron oxide nanoparticles could function as an artificial, inorganic peroxidase. In this paper, we studied the impact of coating on the peroxidase activity of these nanoparticles. Nanoparticles with six different coating structures were synthesized and characterized by FTIR, TGA, TEM, size, zeta potential, and SQUID; and evaluated for peroxidase activity. Catalysis was found to follow Michaelis-Menten kinetics and peroxidase activity varied with respect to electrostatic affinity between nanoparticles and substrates, evidenced by differences in determined kinetic parameters. Glucose detection was selected as a model system because glucose could be indirectly measured from the release of hydrogen peroxide after its oxidation. Nanoparticles with high peroxidase activity exhibited higher sensitivity toward glucose, showing a larger linear slope when compared with those of low activity. A significantly improved linear correlation and detection limit of measured glucose could be readily obtained by manipulating the nanoparticle coating. Our findings suggest that iron oxide nanoparticles can be tailor-made to possess improved peroxidase-like activity. Such enhancements could further widen nanoparticle scope in glucose detection and extend its peroxidase functionality to other biomedical applications. (C) 2009 Elsevier Ltd. All rights reserved.
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