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Redox enzyme-mimicking activities of CeO(2) nanostructures: Intrinsic influence of exposed facets
CeO(2) nanoparticles (NPs) have been well demonstrated as an antioxidant in protecting against oxidative stress-induced cellular damages and a potential therapeutic agent for various diseases thanks to their redox enzyme-mimicking activities. The Ce(3+)/Ce(4+) ratio and oxygen vacancies on the surfa...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5066218/ https://www.ncbi.nlm.nih.gov/pubmed/27748403 http://dx.doi.org/10.1038/srep35344 |
Sumario: | CeO(2) nanoparticles (NPs) have been well demonstrated as an antioxidant in protecting against oxidative stress-induced cellular damages and a potential therapeutic agent for various diseases thanks to their redox enzyme-mimicking activities. The Ce(3+)/Ce(4+) ratio and oxygen vacancies on the surface have been considered as the major originations responsible for the redox enzyme-mimicking activities of CeO(2) NPs. Herein, CeO(2) nanostructures (nanocubes and nanorods) exposed different facets were synthesized via a facile hydrothermal method. The characterizations by X-ray photoelectron spectroscopy, Raman spectroscopy, and UV-Vis spectroscopy show that the Ce(3+)/Ce(4+) ratio and oxygen vacancy content on the surfaces of as-synthesized CeO(2) nanostructures are nearly at the same levels. Meanwhile, the enzymatic activity measurements indicate that the redox enzyme-mimicking activities of as-synthesized CeO(2) nanostructures are greatly dependent on their exposed facets. CeO(2) nanocubes with exposed {100} facets exhibit a higher peroxidase but lower superoxide dismutase activity than those of the CeO(2) nanorods with exposed {110} facets. Our results provide new insights into the redox enzyme-mimicking activities of CeO(2) nanostructures, as well as the design and synthesis of inorganic nanomaterials-based artificial enzymes. |
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