Publications by authors named "Shijiong Wei"

Article Synopsis
  • Formamidopyrimidine DNA glycosylase (FPG) is an important enzyme that repairs DNA by targeting damaged bases like 8-oxoG.
  • A new integrated detection method was developed using magnetic beads, which includes an 8-oxoG probe for FPG recognition and a unique chimeric peptide-DNA mimetic enzyme (CPDzyme) for amplifying signal strength.
  • This method allows for precise detection of FPG activity in a range of 0.2-20 U/mL, with a low detection limit, and has been successfully tested on human serum and bacterial samples, offering a powerful alternative to existing commercial assays.
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Rare earth-doped nanoparticles (RENPs) are promising biomaterials with substantial potential in biomedical applications. Their multilayered core-shell structure design allows for more diverse uses, such as orthogonal excitation. However, the typical synthesis strategies-one-pot successive layer-by-layer (LBL) method and seed-assisted (SA) method-for creating multilayered RENPs show notable differences in spectral performance.

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Biomimetic enzymes have emerged as ideal alternatives to natural enzymes, and there is considerable interest in designing biomimetic enzymes with enhanced catalytic performance to address the low activity of the current biomimetic enzymes. In this study, we proposed a meaningful strategy for constructing an efficient peroxidase-mimicking catalyst, called HhG-MOF, by anchoring histidine (H) and dual hemin-G-quadruplex DNAzyme (double hemin covalently linked to 3' and 5' terminals of G-quadruplex DNA, short as hG) to a mesoporous metal-organic framework (MOF). This design aims to mimic the microenvironment of natural peroxidase.

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Nanomaterials excel in mimicking the structure and function of natural enzymes while being far more interesting in terms of structural stability, functional versatility, recyclability, and large-scale preparation. Herein, the story assembles hemin, histidine analogs, and G-quadruplex DNA in a catalytically competent supramolecular assembly referred to as assembly-activated hemin enzyme (AA-heminzyme). The catalytic properties of AA-heminzyme are investigated both in silico (by molecular docking and quantum chemical calculations) and in vitro (notably through a systematic comparison with its natural counterpart horseradish peroxidase, HRP).

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Given the complexity of the tumor microenvironment, multiple strategies are being explored to tackle hypoxic tumors. The most efficient strategies combine several therapeutic modalities and typically requires the development of multifunctional nanocomposites through sophisticated synthetic procedures. Herein, the G-quadruplex (G4)-forming sequence AS1411-A (d[(G T) TG(TG ) A]) is used for both its anti-tumor and biocatalytic properties when combined with hemin, increasing the production of O ca.

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Biocatalytic transformations in living cells, such as enzymatic cascades, function effectively in spatially confined microenvironments. However, mimicking enzyme catalytic cascade processes is challenging. Herein, we report a new dual-Hemin-G-quadruplex (dHemin-G4) DNAzyme with high catalytic activity over noncovalent G4/Hemin and monocovalent counterparts (G4-Hemin and Hemin-G4) by covalently linking hemin to both ends of an intramolecular G4.

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A high catalytic efficiency associated with a robust chemical structure are among the ultimate goals when developing new biocatalytic systems for biosensing applications. To get ever closer to these goals, we report here on a combination of metal-organic framework (MOF)-based nanozymes and a G-quadruplex (G4)-based catalytic system known as G4-DNAzyme. This approach aims at combining the advantages of both partners (chiefly, the robustness of the former and the modularity of the latter).

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