Carbon Dot Nanozymes: How to Be Close to Natural Enzymes |
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Authors: | Yang Lv Mingrou Ma Prof?Dr Yucheng Huang Prof?Dr Yunsheng Xia |
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Institution: | Key Laboratory of Functional Molecular Solids, Ministry of Education, College of Chemistry and Materials Science, Anhui Normal University, Wuhu, 241000 China |
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Abstract: | The design, catalytic process, and property study of nanozymes are of importance for both fundamental research and application demand. Here, the peroxidase-mimicking properties of a series of carbon dots (C-dots) was systematically investigated and they were found to be probably closer to their natural counterparts, as compared to the known corresponding nanozymes. Firstly, four kinds of metal-free and surface-modulated C-dots were bottom-up fabricated using glucose, α-cyclodextrin (CD), β-CD, and γ-CD as precursors, respectively, and their formation processes, structures, as well as surface chemistry were investigated. Secondly, in the peroxidase-mimicking catalytic system, no hydroxyl radicals were produced, which indicates a different and special catalytic mode. By employing a joint experimental–theoretical study, a probable catalytic mechanism is proposed. Thirdly, the present C-dots maintained well their catalytic activity even in complicated serum matrices because their catalytic performances are completely irrelevant of any cation-related binding sites. Finally, the catalytic performances of the as-prepared C-dots were modulated by either pre-engineering NP surface structures or subsequently introducing photo-regulated host–guest reactions. |
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Keywords: | carbon dots catalysis modulation catalytic mechanism nanozymes peroxidase mimicking |
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