The ethyl celluloses (ECs) modified with 5.0, 10.0, and 20.0 wt % polyaniline (PANI) (PANI/ECs) prepared by homogeneously mixing the EC and PANI formic acid solutions have demonstrated a superior hexavalent chromium (Cr­(VI)) removal performance to that of pure EC. Having an increased Cr­(VI) removal percentage with increased PANI loading, the PANI/ECs with 20.0% PANI loading were noticed to remove 2.0 mg/L Cr­(VI) completely within 5 min, much faster than the pristine EC (>1 h). A chemical redox of Cr­(VI) to Cr­(III) by the active functional groups of PANI/ECs was revealed from the kinetic study. Meanwhile, isothermal study demonstrated a monolayer adsorption behavior following the Langmuir model with a calculated maximum absorption capacity of 19.49, 26.11, and 38.76 mg/g for the 5.0, 10.0, and 20.0 wt % PANI/ECs, much higher than that of EC (12.2 mg/g). The Cr­(VI) removal mechanisms were interpreted considering the functional groups of both PANI and EC, the valence state fates of Cr­(VI), and the variation of solution acidity.

Strong evidence exists for interactions of zwitterionic phosphate and amine groups in sphingosine-1 phosphate (S1P) to conserved Arg and Glu residues present at the extracellular face of the third transmembrane domain of S1P receptors. The contribution of Arg 120 and Glu 121 for high-affinity ligand-receptor interactions is essential, because single-point R 120A or E 121 A S1P 1 mutants neither bind S1P nor transduce S1P function. Because S1P receptors are therapeutically interesting, identifying potent selective agonists with different binding modes and in vivo efficacy is of pharmacological importance. Here we describe a modestly water-soluble highly selective S1P 1 agonist [2-(4-(5-(3,4-diethoxyphenyl)-1,2,4-oxadiazol-3-yl)-2,3-dihydro-1H-inden-1-yl amino) ethanol (CYM-5442)] that does not require Arg 120 or Glu 121 residues for activating S1P 1 -dependent p42/p44 mitogen-activated protein kinase phosphorylation, which defines a new hydrophobic pocket in S1P 1 . CYM-5442 is a full agonist in vitro for S1P 1 internalization, phosphorylation, and ubiquitination. It is noteworthy that CYM-5442 was a full agonist for induction and maintenance of S1P 1 -dependent blood lymphopenia, decreasing B lymphocytes by 65% and T lymphocytes by 85% of vehicle. Induction of CYM-5442 lymphopenia was dose-and time-dependent, requiring serum concentrations in the 50 nM range. In vitro measures of S1P 1 activation by CYM-5442 were noncompetitively inhibited by a specific S1P 1 antagonist [(R)-3-amino-(3-hexylphenylamino)-4-oxobutylphosphonic acid (W146)], competitive for S1P, 2-amino-2-(4-octylphenethyl)propane-1,3-diol (FTY720-P), and 5-[4-phenyl-5-(trifluoromethyl)-2-thienyl]-3-[3-(trifluoromethyl)phenyl]-1,2, 4-oxadiazole (SEW2871). In addition, lymphopenia induced by CYM-5442 was reversed by W146 administration or upon pharmacokinetic agonist clearance. Pharmacokinetics in mice also indicated that CYM-5442 partitions significantly in central nervous tissue. These data show that CYM-5442 activates S1P 1 -dependent pathways in vitro and to levels of full efficacy in vivo through a hydrophobic pocket separate from the orthosteric site of S1P binding that is headgroup-dependent.

Magnetic data storage and magnetically actuated devices are conventionally controlled by magnetic fields generated using electric currents. This involves significant power dissipation by Joule heating effect. To optimize energy efficiency, manipulation of magnetic information with lower magnetic fields (i.e., lower electric currents) is desirable. This can be accomplished by reducing the coercivity of the actuated material. Here, a drastic reduction of coercivity is observed at room temperature in thick (≈600 nm), nanoporous, electrodeposited Cu-Ni films by simply subjecting them to the action of an electric field. The effect is due to voltage-induced changes in the magnetic anisotropy. The large surface-area-to-volume ratio and the ultranarrow pore walls of the system allow the whole film, and not only the topmost surface, to effectively contribute to the observed magnetoelectric effect. This waives the stringent "ultrathin-film requirement" from previous studies, where small voltage-driven coercivity variations were reported. This observation expands the already wide range of applications of nanoporous materials (hitherto in areas like energy storage or catalysis) and it opens new paradigms in the fields of spintronics, computation, and magnetic actuation in general.is conventionally done by localized magnetic fields (generated via electromagnetic induction) or by spin-polarized electric currents (spin-transfer torque). [2,4] Both principles require of relatively high electric currents and therefore involve significant loss of energy in the form of heat dissipation (Joule effect). For example, the currents needed to operate conventional magnetic random-access memories (MRAMs) are of the order of 10 mA, whereas spin-transfer torque MRAMs require currents of at least 0.5 mA. This is still a factor five times larger than the output currents delivered by highly miniaturized metal-oxide-semiconductor field-effect transistors. [5] Replacement of electric currents by electric fields would drastically contribute to reduce the overall power consumption in these and other devices.Several approaches to tailor magnetism by means of an electric field have been proposed so far: (i) strain-mediated magnetoelectric coupling in piezoelectric-magnetostrictive composite materials, [6,7] (ii) multiferroic materials in which the ferroelectric and ferromagnetic order parameters are coupled to each other, [8] and (iii) electric-field induced oxidation-reduction transitions (magnetoionics). [9,10] However, each of these approaches faces some drawbacks, e.g., (i) clamping effects with the substrate, need of epitaxial interfaces, and risk of fatigue-induced mechanical failure; (ii) the dearth of available multiferroic materials and the reduced strength of magnetoelectric coupling, even at low temperatures; and (iii) precise control of the chemical

The mechanism by which locally delivered sphingosine analogs regulate host response to localized viral infection has never been addressed. In this report, we show that intratracheal delivery of the chiral sphingosine analog (R)-2-amino-4-(4-heptyloxyphenyl)-2-methylbutanol (AAL-R) or its phosphate ester inhibits the T-cell response to influenza virus infection. In contrast, neither intraperitoneal delivery of AAL-R nor intratracheal instillation of the nonphosphorylatable stereoisomer AAL-S suppressed virus-specific T-cell response, indicating that in vivo phosphorylation of AAL-R and sphingosine 1-phosphate (S1P) receptor modulation in lungs is essential for immunomodulation. Intratracheal delivery of water-soluble S1P 1 receptor agonist at doses sufficient to induce systemic lymphopenia did not inhibit virus-specific T-cell response, indicating that S1P 1 is not involved in the immunosuppressive activities of AAL-R and that immunosuppression acts independently of naive lymphocyte recirculation. Accumulation of dendritic cells (DCs) in draining lymph nodes was inhibited by intratracheal but not intraperitoneal delivery of AAL-R. Direct modulation of DCs is demonstrated by the impaired ability of virus-infected bone marrow-derived DCs treated in vitro with AAL-R to trigger in vivo T-cell response after adoptive transfer to the airways. Thus, our results suggest that locally delivered sphingosine analogs induce immunosuppression by modulating S1P receptors other than S1P 1 or S1P 2 on dendritic cells in the lungs after influenza virus infection.