Term of Award
Master of Science, Applied Physical Science
Document Type and Release Option
Thesis (open access)
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This work is licensed under a Creative Commons Attribution 4.0 License.
Committee Member 1
Committee Member 2
In this work, nitroxide 2,2,6,6-tetramethylpiperdine 1-oxyl (Tempo), human serum albumin (HSA), CuSO4 and phosphate buffered saline (PBS) were used to synthesis the hybrid nanoflowers. Scanning electron microscopy (SEM), electron paramagnetic resonance (EPR), and Fourier-transform infrared spectroscopy (FTIR) were used for characterization of the nanoflowers.The SEM spectra illustrated the morphologies of the hybrid nanoflowers. The FTIR spectra corroborated the presence of PNA in the hybrid nanoflowers, while the EPR spectra confirmed the intermolecular interaction of nitroxides bound to the human serum albumin incorporated into the nanoflowers. The catalase mimetic activity and corresponding kinetic parameters of nanoflowers were determined using the H2O2 depletion and O2 evolution assays. The superoxide dismutase mimetic activity of the nanoflowers was determined by the xanthine oxidase/cytochrome c method. And the reusability of the hybrid nanoflowers was assessed via the H2O2 depletion assay and the xanthine oxidase/cytochrome c method. Kinetic analysis revealed that the reactions of the incorporated nanoflowers with H2O2 obey Michaelis–Menton kinetics and the nanoflowers possess a higher affinity for H2O2 than nature catalase. the hybrid nanoflowers with superior stability and desired ligand grafting sites will find widespread utilization in the medical sciences.
Cai, Can, "Nitroxide Human Serum Albumin Incorporated Nanoflowers With Dual Enzyme-Like Activities" (2020). Electronic Theses and Dissertations. 2099.
Research Data and Supplementary Material