The synthesis of novel AIE emitters with the triphenylethene-carbazole skeleton and para-/meta-substituted arylboron groups and their application in efficient non-doped OLEDs

Four novel aggregation-induced emission (AIE)-active luminogens (p-DPDECZ, p-DBPDECZ, m-DPDECZ and m-DBPDECZ) with triphenylethene-carbazole skeleton and para-/meta-substituted arylboron groups have been synthesized. Their structures are fully characterized using elemental analysis, mass spectrometry and proton nuclear magnetic resonance spectroscopy. The thermal stabilities, photophysical properties, electronic structures, and electrochemical properties of these molecules are investigated systematically using thermal analysis, UV-vis absorption spectroscopy, fluorescence spectroscopy, theoretical calculation and electrochemical methods. The effects of donor–acceptor interaction and conjugation degree on the photoluminescent and electroluminescent properties of these compounds are investigated. The results show that these donor–AIE–acceptor type compounds exhibit good thermal stability and electrochemical stability as well as AIE properties. Non-doped fluorescent OLEDs fabricated by using para-linked p-DPDECZ as an emitting layer emits a green light with a turn-on voltage of 4.8 V, a maximum brightness of 30210 cd m-2 and a maximum current efficiency of 9.96 cd A-1. While the OLED prepared with meta-linked m-DBPDECZ exhibits efficient blue light emission with a maximum current efficiency of 4.49 cd A-1 and a maximum luminance of 16410 cd m-2. The electroluminescence properties of these compounds demonstrate their potential application in OLEDs

A CATIONIC POLYACRYLAMIDE DISPERSION SYNTHESIS BY DISPERSION POLYMERIZATION IN AQUEOUS SOLUTION

A cationic polyacrylamide (CPAM) dispersion, the copolymer of acrylamide (AM) and acryloyloxyethyltrimethyl ammonium chloride (DAC), has been synthesized through dispersion polymerization in aqueous ammonium sulfate ((NH4)2SO4) solution. The polymerization was initiated by tert-butyl hydroperoxide (TBHP) and ferrisulfas (FeSO4) using poly(dimethyl diallyl ammonium chloride) (PDMDAAC) as the stabilizer. At the optimal reaction conditions, the relative molecular weight of the CPAM dispersion was 4.2×106, its charge density was 2.2 mmol•g-1, its average particle size was 6.01 μm, and its stability and dissolvability were both excellent. The CPAM dispersion was characterized using Fourier-transform infrared (FTIR) spectroscopy, nuclear magnetic resonance (NMR) spectroscopy, and differential scanning calorimeter (DSC). Results indicated that the copolymerization was successful

A Truncated TIR-NBS Protein TN10 Pairs with Two Clustered TIR-NBS-LRR Immune Receptors and Contributes to Plant Immunity in Arabidopsis

The encoding genes of plant intracellular nucleotide-binding site (NBS) and leucine-rich repeat (LRR) domain receptors (NLRs) often exist in the form of a gene cluster. Several recent studies demonstrated that the truncated Toll/interleukin-1 receptor-NBS (TIR-NBS) proteins play important roles in immunity. In this study, we identified a large TN gene cluster on Arabidopsis ecotype Col-0 chromosome 1, which included nine TN genes, TN4 to TN12. Interestingly, this cluster also contained two typical TIR-NBS-LRR genes: At1g72840 and At1g72860 (hereinafter referred to as TNL40 and TNL60, respectively), which formed head-to-head genomic arrangement with TN4 to TN12. However, the functions of these TN and TNL genes in this cluster are still unknown. Here, we showed that the TIR domains of both TNL40 and TNL60 associated with TN10 specifically. Furthermore, both TNL40TIR and TNL60TIR induced cell death in Nicotiana tabacum leaves. Subcellular localization showed that TNL40 mainly localized in the cytoplasm, whereas TNL60 and TN10 localized in both the cytoplasm and nucleus. Additionally, the expression of TNL40, TNL60, and TN10 were co-regulated after inoculated with bacterial pathogens. Taken together, our study indicates that the truncated TIR-NBS protein TN10 associates with two clustered TNL immune receptors, and may work together in plant disease resistanc

Boosting HSA Vaccination with Jujube Powder Modulating Gut Microbiota Favorable for Arginine Metabolism

Whereas vaccination is established as one of the most effective and available methods against seasonal flu and holds high potential for many infectious diseases, immune response may differ among individuals and regions. In this study we examined the effects of gut microbiota on vaccination with human serum albumin (HSA) as the model vaccine in C57BL/6J mice. We observed that a two-week antibiotic cocktail (ABX) treatment hampered HSA-specific IgG1 in serum, whereas fecal microbiota transplantation (FMT) restored the gut microbiota impaired by the ABX treatment and consequently increased the proportions of macrophages in the mesenteric lymph nodes (MLNs), plasma cells in the peripheral blood, and HSA-specific immunoglobulin G1 (IgG1) in the serum. A week of daily application of jujube powder (800 mg/kg) to ABX-treated mice achieved a significantly higher HSA-specific IgG1 concentration in the serum compared with the ABX treatment group. Of particular note was that the administration of the jujube powder did not increase the myeloid cells, indicating a different mechanism of vaccination compared with FMT. More interestingly, daily pre-administration of jujube powder (800 mg/kg) to healthy mice one week ahead of vaccination boosted their immune response, as evidenced by the proportion of macrophages in the MLNs, B cells in the spleen, plasma cells and memory B cells in the peripheral blood, and HSA-specific IgG1 concentration in the serum. The 16S rRNA sequencing of gut microbiota revealed that the administration of jujube powder increased the abundance of Coriobacteriaceae associated with the metabolism of amino acids. The Kyoto encyclopedia of genes and genomes (KEGG) analysis suggested the altered microbiota is more favorable for arginine and proline metabolism, which may promote macrophages in the MLNs. These results indicate a high potential for boosting vaccination by manipulating gut microbiota with natural products

The synthesis, crystal structures, aggregation-induced emission and electroluminescence properties of two novel green-yellow emitters based on carbazole-substituted diphenylethene and dimesitylboron

Introducing the hole-transporting carbazole moiety into an aggregation-induced emissive tetraarylethene skeleton and attaching electron-transporting dimesitylboron groups to the periphery, we obtain two novel electroluminescent materials. Their structures are fully characterized by elemental analysis, mass spectrometry, NMR spectroscopy and X-ray crystallography. Furthermore, their thermal, electrochemical, as well as photophysical properties including AIE-behavior are systematically investigated not only by experimental methods but also by DFT computation. Thereby, we show that the two compounds possess high thermal and electrochemical stability with a remarkable AIE-behavior. X-ray crystal ana- lyses aided by DFT calculations provide insights in the origin of the luminescent properties and AIE features. Ultimately, two non-doped OLEDs (Device A and Device B) were fabricated by using PDPBCE and BDPBCE as light-emitting layer, respectively. Device A showed yellowish-green light with a turn-on voltage of 3.8 V, a maximum brightness of 59130 cd m-2 and a maximum current efficiency of 6.43 cd A -1. Device B exhibited greenish-yellow light with a turn-on voltage of 3.0 V, a maximum brightness of 67,500 cd m-2 and a maximum current efficiency of 11.2 cd A -1

FCHSD1 and FCHSD2 Are Expressed in Hair Cell Stereocilia and Cuticular Plate and Regulate Actin Polymerization <em>In Vitro</em>

<div><p>Mammalian FCHSD1 and FCHSD2 are homologous proteins containing an amino-terminal F-BAR domain and two SH3 domains near their carboxyl-termini. We report here that FCHSD1 and FCHSD2 are expressed in mouse cochlear sensory hair cells. FCHSD1 mainly localizes to the cuticular plate, whereas FCHSD2 mainly localizes along the stereocilia in a punctuate pattern. Nervous Wreck (Nwk), the <i>Drosophila</i> ortholog of FCHSD1 and FCHSD2, has been shown to bind Wsp and play an important role in F-actin assembly. We show that, like its <i>Drosophila</i> counterpart, FCHSD2 interacts with WASP and N-WASP, the mammalian orthologs of <i>Drosophila</i> Wsp, and stimulates F-actin assembly <i>in vitro</i>. In contrast, FCHSD1 doesn’t bind WASP or N-WASP, and can’t stimulate F-actin assembly when tested <i>in vitro</i>. We found, however, that FCHSD1 binds via its F-BAR domain to the SH3 domain of Sorting Nexin 9 (SNX9), a well characterized BAR protein that has been shown to promote WASP-Arp2/3-dependent F-actin polymerization. FCHSD1 greatly enhances SNX9’s WASP-Arp2/3-dependent F-actin polymerization activity. In hair cells, SNX9 was detected in the cuticular plate, where it colocalizes with FCHSD1. Our results suggest that FCHSD1 and FCHSD2 could modulate F-actin assembly or maintenance in hair cell stereocilia and cuticular plate.</p> </div

FCHSD2, but not FCHSD1, binds to WASP and N-WASP and regulates WASP-Arp2/3-mediated F-actin polymerization <i>in vitro</i>.

<p>(A) Western blots showing that FCHSD2, but not FCHSD1, was co-immunoprecipitated with WASP and N-WASP. Expression vectors were transfected into HEK293 cells to express epitope-tagged proteins, and cell lysates were subjected to immunoprecipitation. IP indicates antibody used for immunoprecipitation and WB indicates antibody used for detection. (B) WASP-Arp2/3-mediated F-actin polymerization was enhanced by GST-FCHSD2ΔC, but not by GST-FCHSD1ΔC (or GST). Monomeric actin (3 µM, 10% pyrene-labeled) was incubated with 1 µM GST-FCHSD1ΔC (or GST-FCHSD2ΔC, or GST as control) in the presence of 40 nM His-WASP145 and 20 nM Arp2/3 protein complex, and F-actin polymerization was tracked by monitoring the increase of pyrene fluorescence using a spectrofluorometer. a.u., absorbance units.</p

Improving Electron Mobility of Tetraphenylethene-Based AIEgens to Fabricate Nondoped Organic Light-Emitting Diodes with Remarkably High Luminance and Efficiency

Robust light-emitting materials with strong solid-state fluorescence as well as fast and balanced carrier transporting ability are crucial to achieve high-performance organic light-emitting diodes (OLEDs). In this contribution, two linear tetraphenylethene (TPE) derivatives (TPE-TPAPBI and TPE-DPBI) that are functionalized with hole-transporting triphenylamine and/or electron-transporting 1,2-diphenyl-1<i>H</i>-benzimidazole groups are synthesized and fully characterized. Both TPE-TPAPBI and TPE-DPBI have aggregation-induced emission attributes and excellent photoluminescence quantum yields approaching 100% in vacuum deposited films. They also possess good thermal property, giving high decomposition temperatures (480 and 483 °C) and glass-transition temperatures (141 and 157 °C). TPE-TPAPBI and TPE-DPBI present high electron mobilities of 1.80 × 10^–5 and 1.30 × 10^–4 cm² V ^–1 s^–1, respectively, at an electric field of 3.6 × 10⁵ V cm^–1, which are comparable or even superior to that of 1,3,5-tri­(1-phenylbenzimidazol-2-yl)­benzene. The nondoped OLED device employing TPE-TPAPBI as active layer performs outstandingly, affording ultrahigh luminance of 125 300 cd m^–2, and excellent maximum external quantum, power and current efficiencies of 5.8%, 14.6 lm W^–1, and 16.8 cd A^–1, respectively, with very small roll-offs, demonstrating that TPE-TPAPBI is a highly promising luminescent material for nondoped OLEDs

FCHSD1 and FCHSD2 immunolocalization in mouse cochlear hair cells.

<p>Shown are single confocal sections. FCHSD1 or FCHSD2 immunoreactivity visualized with Cy5 or FITC-conjugated secondary antibody was distinctly associated with stereocilia or cuticular plate, which were visualized with rhodamine-conjugated phalloidin. (A) FCHSD1 immunoreactivity in the cuticular plate of 3-week old mouse cochlear hair cells. (B) FCHSD1 immunoreactivity in the cuticular plate of 3-week old mouse outer hair cells. (C) FCHSD2 immunoreactivity in the hair bundles of 6-week old mouse cochlear hair cells. (D) FCHSD2 immunoreactivity in the hair bundles of 7-month old mouse inner hair cells. (E) FCHSD2 immunoreactivity in the hair bundles of 2-week old mouse outer hair cells. The Novus FCHSD1 antibody was used in (A) and (B). Scale bars: 10 µm in(A-C), 5 µm in (D) and (E).</p

Expression analysis of mouse Fchsd1 and Fchsd2 in different tissues.

<p>(A) Total RNA from postnatal day 5 mouse tissues was extracted and used as template for reverse transcription. PCR was performed using this cDNA as template. Upper panel, <i>Fchsd1</i> mRNA is expressed more abundantly in nervous tissues. Middle panel, <i>Fchsd2</i> mRNA is expressed ubiquitously in all tissues examined. Lower panel, <i>β-actin</i> specific primers were used as the RT-PCR template control. (B) Total proteins of postnatal day 5 mouse cochlea and vestibula were extracted and separated by PAGE and detected with antibodies against FCHSD1(Novus), FCHSD2, or SNX9.</p