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The excessive utilization of antimicrobials in humans and animals has resulted in considerable environmental contamination, necessitating the development of high-performance antibiotic adsorption media. A significant challenge is the development of composite nanofibrous materials that are both beneficial and easy to fabricate, with the aim of improving adsorption capacity. Herein, a new kind of zeolitic imidazolate framework-8 (ZIF-8)-modified regenerated cellulose nanofibrous membrane (ZIF-8@RC NFM) was designed and fabricated by combining electrospinning and in situ surface modification technologies. Benefiting from its favorable surface wettability, enhanced tensile strength, interconnected porous structure, and relatively large specific surface area, the resulting ZIF-8@RC NFMs exhibit a relatively high adsorption capacity for tetracycline hydrochloride (TCH) of 105 mg g−1 within 3 h. Moreover, a Langmuir isotherm model and a pseudo-second-order model have been demonstrated to be more appropriate for the description of the TCH adsorption process of ZIF-8@RC-3 NFMs. Additionally, this composite fibrous material could keep a relatively stable adsorption capability under various ionic strengths. The successful fabrication of the novel ZIF-8@RC NFMs may shed light on the further development of wastewater adsorption treatment materials.

Ceramic fibers have the advantages of high temperature resistance, light weight, favorable chemical stability and superior mechanical vibration resistance, which make them widely used in aerospace, energy, metallurgy, construction, personal protection and other thermal protection fields. Further refinement of the diameter of conventional ceramic fibers to microns or nanometers could further improve their thermal insulation performance and realize the transition from brittleness to flexibility. Processing traditional two-dimensional (2D) ceramic fiber membranes into three-dimensional (3D) ceramic fiber aerogels could further increase porosity, reduce bulk density, and reduce solid heat conduction, thereby improving thermal insulation performance and expanding application areas. Here, a comprehensive review of the newly emerging 2D ceramic micro-nanofiber membranes and 3D ceramic micro-nanofiber aerogels is demonstrated, starting from the presentation of the thermal insulation mechanism of ceramic fibers, followed by the summary of 2D ceramic micro-nanofiber membranes according to different types, and then the generalization of the construction strategies for 3D ceramic micro-nanofiber aerogels. Finally, the current challenges, possible solutions, and future prospects of ceramic micro-nanofiber materials are comprehensively discussed. We anticipate that this review could provide some valuable insights for the future development of ceramic micro-nanofiber materials for high temperature thermal insulation.

Nanofibrous materials are considered as promising candidates for fabricating high-efficiency chromatography media, which are urgently needed in protein pharmaceuticals purification and biological research, yet still face several bottlenecks. Herein, novel negatively charged composite nanofibrous hydrogel membranes (NHMs) are obtained by a facile combination of electrospinning and surface coating modification. The resulting NHMs exhibit controllable morphologies and chemical structures. Benefitting from the combined effect of the stable framework of silicon dioxide (SiO2) nanofiber and the function layer of negatively charged hydrogel, as well as good pore connectivity among nanofibers, NHMs exhibit a high protein adsorption capacity of around 1000 mg g−1, and are superior to the commercial cellulose fibrous adsorbent (Sartobind®) and the reported nanofibrous membranous adsorbents. Moreover, due to their relatively stable physicochemical and mechanical properties, NHMs possess comprehensive adsorption performance, favorable resistance to acid and solvents, good selectivity, and excellent regenerability. The designed NHMs composite adsorbents are expected to supply a new protein chromatography platform for effective protein purification in biopharmaceuticals and biochemical reagents.

Abstract Background Homoharringtonine (HHT) is a natural alkaloid with potent antitumor activity, but its precise mechanism of action is still poorly understood. Methods We examined the effect of HHT on alternative splicing of Bcl-x and Caspase 9 in various cells using semi-quantitative reverse transcriptase-polymerase chain reaction (RT-PCR). The mechanism of HHT-affected alternative splicing in these cells was investigated by treatment with protein phosphatase inhibitors and overexpression of a protein phosphatase. Results Treatment with HHT downregulated the levels of anti-apoptotic Bcl-xL and Caspase 9b mRNA with a concomitant increase in the mRNA levels of pro-apoptotic Bcl-xS and Caspase 9a in a dose- and time-dependent manner. Calyculin A, an inhibitor of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A), significantly inhibited the effects of HHT on the alternative splicing of Bcl-x and Caspase 9, in contrast to okadaic acid, a specific inhibitor of PP2A. Overexpression of PP1 resulted in a decrease in the ratio of Bcl-xL/xS and an increase in the ratio of Caspase 9a/9b. Moreover, the effects of HHT on Bcl-x and Caspase 9 splicing were enhanced in response to PP1 overexpression. These results suggest that HHT-induced alternative splicing of Bcl-x and Caspase 9 is dependent on PP1 activation. In addition, overexpression of PP1 could induce apoptosis and sensitize MCF7 cells to apoptosis induced by HHT. Conclusion Homoharringtonine regulates the alternative splicing of Bcl-x and Caspase 9 through a PP1-dependent mechanism. Our study reveals a novel mechanism underlying the antitumor activities of HHT.

The identification and quantitative analysis of protein-protein interactions are essential to the functional characterization of proteins in the post-proteomics era. The methods currently available are generally time-consuming, technically complicated, insensitive and/or semi-quantitative. The lack of simple, sensitive approaches to precisely quantify protein-protein interactions still prevents our understanding of the functions of many proteins. Here, we develop a novel dual luciferase reporter pull-down assay by combining a biotinylated Firefly luciferase pull-down assay with a dual luciferase reporter assay. The biotinylated Firefly luciferase-tagged protein enables rapid and efficient isolation of a putative Renilla luciferase-tagged binding protein from a relatively small amount of sample. Both of these proteins can be quantitatively detected using the dual luciferase reporter assay system. Protein-protein interactions, including Fos-Jun located in the nucleus; MAVS-TRAF3 in cytoplasm; inducible IRF3 dimerization; viral protein-regulated interactions, such as MAVS-MAVS and MAVS-TRAF3; IRF3 dimerization; and protein interaction domain mapping, are studied using this novel assay system. Herein, we demonstrate that this dual luciferase reporter pull-down assay enables the quantification of the relative amounts of interacting proteins that bind to streptavidin-coupled beads for protein purification. This study provides a simple, rapid, sensitive, and efficient approach to identify and quantify relative protein-protein interactions. Importantly, the dual luciferase reporter pull-down method will facilitate the functional determination of proteins.