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1.
J Colloid Interface Sci ; 628(Pt A): 717-725, 2022 Dec 15.
Artículo en Inglés | MEDLINE | ID: mdl-35944302

RESUMEN

Most biochemical reactions that occur in living organisms are catalyzed by a series of enzymes and proceed in a tightly controlled manner. The development of artificial enzyme cascades that resemble multienzyme complexes in nature is of current interest due to their potential in various applications. In this study, a nanozyme based on photoswitchable carbon-dot liposomes (CDsomes) was developed for use in programmable catalytic cascade reactions. These CDsomes prepared from triolein are amphiphilic and self-assemble into liposome-like structures in an aqueous environment. CDsomes feature excitation-dependent photoluminescence and, notably, can undergo reversible switching between a fluorescent on-state and nonfluorescent off-state under different wavelengths of light irradiation. This switching ability enables the CDsomes to exert photocatalytic oxidase- and peroxidase-like activities in their on- (bright) and off- (dark) states, respectively, resulting in the conversion of oxygen molecules into hydrogen peroxide (H2O2), followed by the generation of active hydroxyl radicals (OH). The two steps of oxygen activation can be precisely controlled in a sequential manner by photoirradiation at different wavelengths. Catalytic reversibility also enables the CDsomes to produce sufficient reactive oxygen species (ROS) to effectively kill tumor cells. Our results reveal that CDsomes is a promising photo-cycling nanozyme for precise tumor phototherapy through regulated programmable cascade reactions.


Asunto(s)
Peróxido de Hidrógeno , Liposomas , Carbono , Catálisis , Complejos Multienzimáticos/química , Oxidorreductasas , Oxígeno , Peroxidasas , Especies Reactivas de Oxígeno , Trioleína
2.
Anal Biochem ; 608: 113844, 2020 11 01.
Artículo en Inglés | MEDLINE | ID: mdl-32763304

RESUMEN

In this work, a colorimetric aptamer-based method for detection of cadmium using gold nanoparticles modified MoS2 nanocomposites as enzyme mimic is established. In short, biotinylated Cd2+ aptamers are immobilized by biotin-avidin binding on the bottoms of the microplate, the complementary strands of Cd2+ aptamers are connected to the Au-MoS2 nanocomposites which have the function of enhanced peroxidase-like activity. The csDNA-Au-MoS2 signal probe and target Cd2+ compete for binding Cd2+ aptamer, the color change can be observed by addition of chromogenic substrate, thereby realizing visual detection of Cd2+. The absorbance of the solution at 450 nm has a clear linear relationship with the Cd2+ concentration. The linear range is 1-500 ng/mL, and the limit of detection is 0.7 ng/mL. The assay was used to test white wine samples, the results are consistent with those of atomic absorption spectrometry; which prove that this method can be used for detection of Cd2+ in real samples.


Asunto(s)
Aptámeros de Nucleótidos/química , Cadmio/análisis , Cadmio/química , Cationes Bivalentes/análisis , Cationes Bivalentes/química , Colorimetría/métodos , Nanocompuestos/química , Compuestos Cromogénicos/química , ADN Complementario/síntesis química , ADN Complementario/química , Disulfuros/química , Pruebas de Enzimas/métodos , Oro/química , Microscopía Electrónica de Transmisión , Molibdeno/química , Oxidación-Reducción , Peroxidasas/química , Espectrofotometría , Vino/análisis , Difracción de Rayos X
3.
In Vitro Cell Dev Biol Anim ; 54(5): 335-345, 2018 May.
Artículo en Inglés | MEDLINE | ID: mdl-29560557

RESUMEN

The balance of oxidation and reduction in the body requires the synergistic effect of various antioxidant enzymes. Therefore, the construction of enzyme mimics with multiple antioxidant activities is important and beneficial for further research on the synergistic effects of antioxidant enzymes and their mechanism of action. To explore the synergistic effect of superoxide dismutase (SOD) and glutathione peroxidase (GPx), a 76-mer selenium-containing peptide (Se-76P) mimic containing the active SOD and GPx centers was designed. Moreover, a cell-penetrating peptide was introduced into Se-76P by structure modeling, and then, Se-76P was expressed by a single-protein production combined with the cysteine auxotrophic double-expression system of Escherichia coli. The results suggest that Se-76P exhibits SOD and GPx activities, following the GPx activity of 109 U/mg protein and the SOD activity of 1218 U/mg protein. The labeled Se-76P with FITC fluorescence was verified to enter the L02 cells successfully; it improved the antioxidant activity in cells and promoted the consumption of glucose and synthesis of glycogen. The injection of Se-76P subcutaneously decreased the levels of blood glucose and malondialdehyde of lipid peroxidation produced in mice, indicating that Se-76P had antioxidative properties and a certain regulatory role of glucose metabolism. The data analysis provides further clarification that Se-76P can regulate insulin signal transduction to play an insulin-like role, which not only has a greater significance for further elucidating the catalytic mechanism of the enzyme and their synergistic effects on each other but also has enormous medicinal potential.


Asunto(s)
Péptidos de Penetración Celular/química , Insulina/metabolismo , Peroxidación de Lípido/efectos de los fármacos , Péptidos/química , Antioxidantes/química , Antioxidantes/metabolismo , Metabolismo de los Hidratos de Carbono/genética , Dominio Catalítico/efectos de los fármacos , Péptidos de Penetración Celular/farmacología , Glucosa/metabolismo , Glutatión Peroxidasa/química , Humanos , Insulina/química , Oxidación-Reducción/efectos de los fármacos , Péptidos/genética , Péptidos/farmacología , Selenio/química , Superóxido Dismutasa/química
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