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Título: | Enzyme/Nanocopper Hybrid Nanozymes: Modulating Enzyme-like Activity by the Protein Structure for Biosensing and Tumor Catalytic Therapy |
Autor: | Losada-Garcia, Noelia; Jiménez-Alesanco, Ana CSIC; Velázquez-Campoy, Adrián; Abian, Olga CSIC ORCID; Palomo, José Miguel | Palabras clave: | Nanozymes Copper hybrids Nanoparticles Oxidase-like activity Biosensors Cytotoxicity |
Fecha de publicación: | 20-ene-2021 | Editor: | American Chemical Society | Citación: | ACS Applied Materials and Interfaces 13: 5111-5124 (2021) | Resumen: | Artificial enzymes with modulated enzyme-mimicking activities of natural systems represent a challenge in catalytic applications. Here, we show the creation of artificial Cu metalloenzymes based on the generation of Cu nanoparticles in an enzyme matrix. Different enzymes were used, and the structural differences between the enzymes especially influenced the controlled the size of the nanoparticles and the environment that surrounds them. Herein, we demonstrated that the oxidase-like catalytic activity of these copper nanozymes was rationally modulated by enzyme used as a scaffold, with a special role in the nanoparticle size and their environment. In this sense, these nanocopper hybrids have confirmed the ability to mimic a unique enzymatic activity completely different from the natural activity of the enzyme used as a scaffold, such as tyrosinase-like activity or as Fenton catalyst, which has extremely higher stability than natural mushroom tyrosinase. More interestingly, the oxidoreductase-like activity of nanocopper hybrids was cooperatively modulated with the synergistic effect between the enzyme and the nanoparticles improving the catalase activity (no peroxidase activity). Additionally, a novel dual (metallic and enzymatic activity) of the nanozyme made the highly improved catechol-like activity interesting for the design of 3,4-dihydroxy-l-phenylalanine (l-DOPA) biosensor for detection of tyrosinase. These hybrids also showed cytotoxic activity against different tumor cells, interesting in biocatalytic tumor therapy. | Descripción: | 14 pags., 12 figs., 1 tab. | Versión del editor: | http://dx.doi.org/10.1021/acsami.0c20501 | URI: | http://hdl.handle.net/10261/248474 | DOI: | 10.1021/acsami.0c20501 | Identificadores: | doi: 10.1021/acsami.0c20501 issn: 1944-8252 |
Aparece en las colecciones: | (IQF) Artículos (ICP) Artículos |
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