4 research outputs found

    Visible-Light-Induced Self-Cleaning Property of Bi<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub>‑TiO<sub>2</sub> Composite Nanowire Arrays

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    Bi<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub>-TiO<sub>2</sub> composite nanowire arrays were prepared via a two-step sequential solvothermal and subsequent calcination process. The morphology and structure of the Bi<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub>-TiO<sub>2</sub> composite nanowire array composite were characterized by X-ray diffraction, field emission scanning electron microscopy, and transmission electron microscopy. The UV–visible diffuse reflectance spectroscopy analysis indicated that the absorption spectrum of the Bi<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub>-TiO<sub>2</sub> composite nanowire array composite was extended to the visible-light region due to the existence of Bi<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub>. The Bi<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub>-TiO<sub>2</sub> composite nanowire arrays exhibit superhydrophilicity with water contact angles of 0° after irradiation with visible light, and the superhydrophilic nature is retained for at least 15 days. This effect enables us to consider self-cleaning applications that do not require permanent UV exposure. Compared to pure Bi<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub> and TiO<sub>2</sub>, the vertically aligned Bi<sub>2</sub>Ti<sub>2</sub>O<sub>7</sub>-TiO<sub>2</sub> composite nanowire arrays showed more significant visible-light self-cleaning performance due to the synergistic effect of superhydrophilicity and significant photocatalytic activity caused by effective electron–hole separation at the interfaces of the two semiconductors, which was confirmed by the electrochemical analysis and surface photovoltage technique

    Detailed Glycan Structural Characterization by Electronic Excitation Dissociation

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    The structural complexity and diversity of glycans parallel their multilateral functions in living systems. To better understand the vital roles glycans play in biological processes, it is imperative to develop analytical tools that can provide detailed glycan structural information. This was conventionally achieved by multistage tandem mass spectrometry (MS<sup>n</sup>) analysis using collision-induced dissociation (CID) as the fragmentation method. However, the MS<sup>n</sup> approach lacks the sensitivity and throughput needed to analyze complex glycan mixtures from biological sources, often available in limited quantities. We define herein the critical parameters for a recently developed fragmentation technique, electronic excitation dissociation (EED), which can yield rich structurally informative fragment ions during liquid chromatographic (LC)-MS/MS analysis of glycans. We further demonstrate that permethylation, reducing end labeling and judicious selection of the metal charge carrier, can greatly facilitate spectral interpretation. With its high sensitivity, throughput, and compatibility with online chromatographic separation techniques, EED appears to hold great promise for large-scale glycomics studies

    Hierarchical Core–Shell Carbon Nanofiber@ZnIn<sub>2</sub>S<sub>4</sub> Composites for Enhanced Hydrogen Evolution Performance

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    Improvement of hydrogen evolution ability is an urgent task for developing advanced catalysts. As one of the promising visible-light photocatalysts, ZnIn<sub>2</sub>S<sub>4</sub> suffers from the ultrafast recombination of photoinduced charges, which limits its practical application for efficient solar water splitting. Herein, we reported a two-step method to prepare hierarchical core–shell carbon nanofiber@​ZnIn<sub>2</sub>S<sub>4</sub> composites. One-dimensional carbon nanofibers were first prepared by electrospinning and carbonization in N<sub>2</sub>. The subsequent solvothermal process led to the in situ growth of ZnIn<sub>2</sub>S<sub>4</sub> nanosheets on the carbon nanofibers to fabricate hierarchical structure composites. The hierarchical core–shell configuration structure can help to form an intimate contact between the ZnIn<sub>2</sub>S<sub>4</sub> nanosheet shell and the carbon nanofiber backbone compared with the equivalent physical mixture and can facilitate the interfacial charge transfer driven by the excitation of ZnIn<sub>2</sub>S<sub>4</sub> under visible-light irradiation. Meanwhile, the ultrathin ZnIn<sub>2</sub>S<sub>4</sub> nanosheets were uniformly grown on the surface of the carbon nanofibers, which can avoid agglomeration of ZnIn<sub>2</sub>S<sub>4</sub>. These synergistic effects made this unique hierarchical structure composite exhibit a significantly higher visible-light photocatalytic activity toward hydrogen evolution reaction compared with pure ZnIn<sub>2</sub>S<sub>4</sub> or a physical mixture of ZnIn<sub>2</sub>S<sub>4</sub> and carbon nanofibers in the absence of noble metal cocatalysts

    Agonist-Activated <i>Bombyx</i> Corazonin Receptor Is Internalized via an Arrestin-Dependent and Clathrin-Independent Pathway

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    Agonist-induced internalization plays a key role in the tight regulation of the extent and duration of G protein-coupled receptor signaling. Previously, we have shown that the <i>Bombyx</i> corazonin receptor (BmCrzR) activates both G<sub>αq</sub>- and G<sub>αs</sub>-dependent signaling cascades. However, the molecular mechanisms involved in the regulation of the internalization and desensitization of BmCrzR remain to be elucidated. Here, vectors for expressing BmCrzR fused with enhanced green fluorescent protein (EGFP) at the C-terminal end were used to further characterize BmCrzR internalization. We found that the BmCrzR heterologously expressed in HEK-293 and BmN cells was rapidly internalized from the plasma membrane into the cytoplasm in a concentration- and time-dependent manner via a β-arrestin (Kurtz)-dependent and clathrin-independent pathway in response to agonist challenge. While most of the internalized receptors were recycled to the cell surface via early endosomes, some others were transported to lysosomes for degradation. Assays using RNA interference revealed that both GRK2 and GRK5 were essentially involved in the regulation of BmCrzR phosphorylation and internalization. Further investigations indicated that the identified cluster of Ser/Thr residues (<sup>411</sup>TSS<sup>413</sup>) was responsible for GRK-mediated phosphorylation and internalization. This is the first detailed investigation of the internalization and trafficking of <i>Bombyx</i> corazonin receptors
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