Successful synthesis of room-temperature ferromagnetic semiconductors, Zn$_{1-x}$Fe$_{x}$O, is reported. The essential ingredient in achieving room-temperature ferromagnetism in bulk Zn$_{1-x}$Fe$_{x}$O was found to be additional Cu doping. A transition temperature as high as 550 K was obtained in Zn$_{0.94}$Fe$_{0.05}$Cu$_{0.01}$O; the saturation magnetization at room temperature reached a value of $0.75 \mu_{\rm B}$ per Fe. Large magnetoresistance was also observed below $100 $K.Comment: 11 pages, 4 figures; to appear in Appl. Phys. Let

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Chrysin is a natural, biologically active compound extracted from many plants, honey and propolis. It possesses potent anti-inflammation, anti-cancer and anti-oxidation properties. The mechanism by which chrysin suppresses COX-2 expression remains poorly understood. In the present report, we investigated the effect of chrysin on the expression of COX-2 in lipopolysaccharide (LPS)-activated Raw 264.7 cells. Chrysin significantly suppressed the LPS-induced COX-2 protein and mRNA expression in a dose-dependent manner. The ability of chrysin to suppress the expression of the COX-2 was investigated using luciferase reporters controlled by various cis-elements in COX-2 promoter region. Mutational analysis and electrophoretic mobility shift assay verified that nuclear factor for IL-6 was identified as responsible for the chrysin-mediated COX-2 downregulation. These results will provide new insights into the anti-inflammatory and anti-carcinogenic properties of chrysin.

Contrasting magnetic properties were obtained from bulk Mn-doped ZnO synthesized under different processing conditions. While a ferrimagnetic phase transition was observable in a Zn0.95Mn0.05O sample processed at 1170 K, no such transition was found for a sample with the same composition processed at 1370 K. The detailed magnetic, structural, and spectroscopic studies of these two samples have revealed that the ferrimagnetic transition in the former sample is attributable to the secondary phase, (Mn,Zn)Mn2O4, in the system. For the latter sample processed at higher temperature, no secondary phase was detected and the major feature of the system remained paramagnetic down to 4 K. The implication of the present results for Mn-doped ZnO thin films is discussed.

Fe- and Cu-codoped ZnO was previously reported as a room-temperature dilute magnetic semiconductor. We have investigated the origin of the ferromagnetism in Zn0.95−xFe0.05CuxO using the zero-field Fe57 nuclear magnetic resonance and neutron diffraction. These measurements reveal that some Fe ions of Zn0.95−xFe0.05CuxO form a secondary phase, ZnFe2O4. Detailed comparison of nuclear magnetic resonance spectra of Zn0.95−xFe0.05CuxO, bulk ZnFe2O4 with normal spinel structure, and nanocrystalline ZnFe2O4 with inverted spinel structure shows that the secondary phase possesses an inverted spinel structure and is ferrimagnetic at room temperature, while normal zinc ferrite is nonmagnetic. The ferromagnetism in Fe- and Cu-codoped ZnO stems from the secondary phase, while the majority of Fe ions substituted into the ZnO lattice appears to remain magnetically inert.

Shell cross-linked hollow polyelectrolyte microcapsules composed of hyaluronic acid (HA) and poly- l-lysine (PLL) were prepared by layer-by-layer (LBL) adsorption and subsequent core removal by a reductive agent. Disulfide cross-linked HA microgels were used as template core materials for the LBL deposition on the surface and removed by treatment of dithiothreitol at neutral pH condition. HA/PLL polyelectrolyte multilayers on the shell were chemically cross-linked via carbodiimide chemistry, and their physicochemical properties and drug release behaviors were investigated. Shell cross-linked HA/PLL polyelectrolyte microcapsules exhibited far enhanced physical stability against freeze-thaw cycles and acidic pH conditions compared to the un-cross-linked ones. The cross-linked HA/PLL multilayer shell also demonstrated pH responsive permeability, which became more permeable at low pH than at neutral pH. When bovine serum albumin (BSA), as a model protein drug, was loaded inside using the pH-dependent permeability, BSA release profiles from the microcapsules could be readily modulated by varying medium pH values or adding an HA digesting enzyme (hyaluronidase) in the incubation medium.

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