Catalytic Cracking of Supercritical <i>n</i>‑Dodecane over Wall-Coated Nano-Ag/HZSM‑5 Zeolites

A series of Ag modified zeolites were prepared by incipient impregnation of nano-HZSM-5 with AgNO₃ (0.5–2.0 wt %) aqueous solutions. It was found that the ion-exchange and impregnation effect both existed in this impregnation process, resulting in the formation of various silver species which altered the zeolite acid properties. The wall-coated nano-Ag/HZSM-5 zeolites were prepared on the inner surface of 304 stainless steel tubes though the washcoating method. Catalytic cracking of supercritical <i>n</i>-dodecane (4 MPa, 550 °C) was used to examine the catalytic activities of the prepared catalytic coatings. It is found that the modified samples with 1.0% Ag showed higher conversion (up to 1.50 times) than the parent one because of the dehydrogenation effect of silver species and that the overloaded (for example, 2.0 wt %) samples show lower performances ascribing to the blockage of diffusion pores by the silver species

Balancing Compatibility and Gelability for High-Performance Cholesteric Liquid Crystalline Physical Gels

Liquid crystalline physical gels (LCPGs) have attracted increasing interest because of their mechanical properties and stimulus–response behaviors. However, due to their gelator properties such as thermal stability, gelation capability, and compatibility in liquid crystals, development of LCPGs with high performances still remains a huge challenging task. Herein, four novel gelators ((l)-PH, (d)-PH, (l)-P2H, and (d)-P2H) based on 1,4-benzenedicarboxamide phenylalanine derivatives containing one or two ethylene glycol groups have been designed and synthesized. It is found that the ethylene glycol group plays a significant role in improving the compatibility between the gelator and the liquid crystal. All of the prepared compounds can form stable LCPGs in P0616A. In particular, the storage modulus of LCPG with 9.0 wt % of (l)-PH with one ethylene glycol unit is higher than 106 Pa, which is similar to SmC gels and advantageous over previously reported nematic LCPGs. Furthermore, the prepared gels display a strong Cotton effect with hand-preferred twisted fiber networks and the self-assembled aggregates of (l)-PH can induce P0616A to form a cholesteric fingerprint structure. Thus, these low molecular weight gelators provide a strategy to construct high-performance cholesteric LCPGs for the realization of LC device applications

The ability of all of the TLR2 mutants to recruit MyD88.

<p>HEK293T cells were co-transfected with empty vector pFLAG-CMV8, FLAG-tagged wild-type TLR2 or each of the TLR2 mutants, along with MyD88-HA. At 24 h post-transfection, the cells were stimulated with LTA, Pam3CSK4 or FSL for 30 min. The cells were lysed, and the extracts were immunoprecipitated by anti-FLAG conjugated beads. TLR2 and MyD88 were subsequently detected in the immunoprecipitated proteins by western blot with an anti-FLAG antibody and an anti-HA polyclonal antibody. The quantity of MyD88 in the whole cell lysates was also detected with the anti-HA polyclonal antibody. The experiment was repeated for three times, and one was represented.</p

Electrostatic charge and conformation of the BB and CD loop were compared between wild-type TLR2 and its mutants.

<p>A, the conformation of the BB and CD loop in wild-type TLR2, TLR2 (L663E), TLR2 (P681A) and TLR2 (N688A) was compared, and the mutated residues L663E, P681A and N688A were stick represented. B, comparison of the electrostatic surfaces of wild-type TLR2, TLR2 (L663E), TLR2 (P681A) and TLR2 (N688A), the change of positive charge (<i>blue</i>) and negative charge (<i>red</i>) in the BB loop was indicated by a circle, and the mutated residues L663E, P681A and N688A were indicated by an arrow.</p

Expression and intracellular distribution of the human TLR2 mutants.

<p>HEK293T cells in 24-well plates were transfected with each indicated mutant and analysed 24 h later. A, the cells were stained with FITC-labelled anti-FLAG and DAPI and observed under confocal fluorescence microscopy. B, the surface expression of wild-type TLR2 (<i>solid line</i>) and each of the TLR2 mutants (<i>thin line</i>) on HEK293 was detected by FACS. C, the expression of wild-type TLR2 (<i>solid line</i>) and each of the TLR2 mutants (<i>thin line</i>) was detected following permeabilisation of the cell membrane. D, the expression of each of the TLR2 mutants was determined by western blot, with β-actin as an internal control. Each experiment was repeated for three times, and one was represented.</p

Responsiveness of human TLR2 (N657E), TLR2 (L663E) and TLR2 (N688A) to TLR2/2, TLR2/1 and TLR2/6 agonists.

<p>HEK293T cells in 24-well plates were transfected with human TLR2 (N657E), TLR2 (L663E) or TLR2 (N688A), and TK-RL and pBIIx-luc. At 24 h post-transfection, the cells were stimulated with the indicated concentrations of LTA (A), Pam3CSK4 (B) and FSL (C) for 6 h, respectively, and then both firefly and Renilla luciferase activities were determined using a dual-luciferase assay. The experiments were repeated for three times, and all of the data were expressed as the mean ± SD. * indicated as <i>p</i><0.05.</p

Responsiveness of human TLR2 (P681A) to TLR2/2, TLR2/1 and TLR2/6 agonists.

<p>HEK293T cells in 24-well plates were transfected with TLR2 (P681A), TK-RL and pBIIx-luc. At 24 h post-transfection, the cells were stimulated with the indicated concentrations of LTA (A), Pam3CSK4 (B) and FSL (C) for 6 h, respectively, and then both firefly and Renilla luciferase activities were determined using a dual-luciferase assay. The experiments were repeated for three times, and all of the data were expressed as the mean ± SD. *<i>P</i><0.05, ** <i>P</i><0.01, ns, not significant.</p

Conserved amino acid residues in all but not human TLR3 TIR domain and their location in the crystal structure of human TLR2 TIR.

<p>A, All of the TIR domains, including human TLR2, TLR3, TLR1, TLR6, TLR4, TLR5, TLR7, TLR8,TLR9 and TLR10, were aligned. The sequences responsible for the structure of αA, βA, αB, and the amino acid residues specific for human TLR3 TIR and one (657 E) specific for TLR3, but semi-conserved in all other human TLRs TIRs were underlined. The BB loop was indicated as the sequence between βA and αB, and three conserved amino acid residues in all of the TLRs, except for the TLR3 TIR domain, such as L, P and N, were indicated as“*”. The numbers indicate the positions of the amino acid residues in human TLR2. B, Stick representation of all three conserved amino acid Leu (663), Pro (681) and Asn (688), and highlighting BB loop (<i>pink</i>) in the cystal structure of human TLR2 TIR domain.</p

Additional file 1: of SGEF is a potential prognostic and therapeutic target for lung adenocarcinoma

Figure S1. The schematic of the SGEF protein structure. Full length of SGEF protein contains an amino-terminal proline-rich region (Pro), a Dbl homology (DH) domain, and pleckstrin homology (PH) domain, as well as Src homology 3 domain (SH3). (TIFF 58 kb

Precisely Tuning Helical Twisting Power via Photoisomerization Kinetics of Dopants in Chiral Nematic Liquid Crystals

It has been paid much attention to improve the helical twisting power (β) of dopants in chiral nematic liquid crystals (CLCs); however, the correlations between the β value and the molecular structures as well as the interaction with nematic LCs are far from clear. In this work, a series of reversibly photo-switchable axially chiral dopants with different lengths of alkyl or alkoxyl substituent groups have been successfully synthesized through nucleophilic substitution and the thiol–ene click reaction. Then, the effect of miscibility between these dopants and nematic LCs on the β values, as well as the time-dependent decay/growth of the β values upon irradiations, has been investigated. The theoretical Teas solubility parameter shows that the miscibility between dopants and nematic LCs decreases with increasing of the length of substituent groups from dopant <b>1</b> to dopant <b>4</b>. The β value of chiral dopants in nematic LCs decreases from dopant <b>1</b> to dopant <b>4</b> both at the visible light photostationary state (PSS) and at the UV PSS after UV irradiation. With increasing of the length of substituent groups, the photoisomerization rate constant of dopants increases for trans–cis transformation upon UV irradiation and decreases for the reverse process upon visible light irradiation either in isotropic ethyl acetate or in anisotropic LCs, although the constant in ethyl acetate is several times larger than the corresponding value in LCs. Also, the color of the CLCs could be tuned upon light irradiations. These results enable the precise tuning of the pitch and selective reflection wavelength/color of CLCs, which paves the way to the applications in electro-optic devices, information storage, high-tech anticounterfeit, and so forth