Sol-gel synthesis of ZnO/Zn<Subscript>2-x</Subscript>Fe<Subscript>x</Subscript>TiO<Subscript>4</Subscript> powders: structural properties,electrical conductivity and dielectric behavior

The aim of this work was an investigation of structural and electrical properties of ZnO/Zn_2-xFe_xTiO₄ (x?=?0.7, 1, 1.4) powders. The compounds obtained by sol-gel method are characterized by several techniques: X-ray diffraction (XRD), N₂ adsorption–desorption isotherms, scanning and transmission electron microscopy (SEM and TEM), X-ray photoelectron spectroscopy (XPS), electrical and dielectrical measurements. The XRD, SEM and XPS analysis confirmed the formation of ZnFeTiO₄ inverse spinel structure. The electrical and dielectrical properties of ZnO/Zn_2-xFe_xTiO₄ (x?=?0.7, 1, 1.4) were measured by impedance spectroscopy, revealing a decrease in the electrical conductivity and the dielectric constant with Fe content.

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Mass spectrometric approaches for elucidation of antigenantibody recognition structures in molecular immunology

Mass spectrometric approaches have recently gained increasing access to molecular immunology and several methods have been developed that enable detailed chemical structure identification of antigen-antibody interactions. Selective proteolytic digestion and MS-peptide mapping (epitope excision) has been successfully employed for epitope identification of protein antigens. In addition, "affinity proteomics" using partial epitope excision has been developed as an approach with unprecedented selectivity for direct protein identification from biological material. The potential of these methods is illustrated by the elucidation of a beta-amyloid plaque-specific epitope recognized by therapeutic antibodies from transgenic mouse models of Alzheimer's disease. Using an immobilized antigen and antibody-proteolytic digestion and analysis by high resolution Fourier transform ion cyclotron resonance mass spectrometry has lead to a new approach for the identification of antibody paratope structures (paratope-excision; "parex-prot"). In this method, high resolution MS-peptide data at the low ppm level are required for direct identification of paratopes using protein databases. Mass spectrometric epitope mapping and determination of "molecular antibody-recognition signatures" offer high potential, especially for the development of new molecular diagnostics and the evaluation of new vaccine lead structures.     

Novel UV assay for protein determination and the characterization of copper-protein complexes by mass spectrometry

A very simple, highly selective and sensitive assay of proteins based on the biuret absorption in the ultraviolet region has been developed. The well-known biuret assay is based on the reaction of proteins with copper ions under strong alkaline conditions to form a copper-protein complex. Yet, copper ions may seriously interfere with the determination if the measurement is made in the UV range. In the present approach, proteins mobilize copper ions from insoluble salts at different pH values, and the copper-protein complexes are investigated by UV spectrophotometry and mass spectrometry. Upon using copper phosphate, free copper ions do not interfere with the determination from 540 to 240 nm. Copper absorbance slowly increases from 240 to 190 nm where a blank with the reagents is recommended. A maximum absorbance for the copper-protein complex was found at 226 nm and high pH value. The stoichiometries of the copper-protein complexes measured directly with a mass spectrometer are pH dependent: half of the peptides without any histidine residue chelate just a single Cu²⁺ ion at pH 7.4 but each such peptide mobilizes from 1 to 6 Cu²⁺ ions at pH 10.3. To determine proteins, 1-1.5 ml of 1.8% KOH solution with 0-20 μg ml⁻¹ protein is treated with 25 mg of copper phosphate powder. The mixture is powerfully stirred, centrifuged, and the absorbance of the supernatant is measured at 226 nm in 1 cm quartz cuvettes against a blank of the reagents. The color system obeys Beer's law in the range 0.1-20 μg ml⁻¹ protein at this wavelength. The molar absorptivity value proved to be a characteristic of each protein being analyzed. Therefore, individual proteins should be used to plot calibration curves. This assay proved to be over 100 times more sensitive than the classical biuret procedure. The method is highly selective and the determination is little affected by the presence of other substances. All other important analytical parameters were studied and practical applicability of the method has been verified by the analysis of some biological materials.     

Permethylated dinuclear Mn(III) coordination nanostructure with stripe-ordered magnetic domains

A di-manganese(III) complex structure was built by an original approach consisting of a two-step procedure. First, the mononuclear complex of the manganese(III) with the Schiff base of the salen-type ligand (H₂L) derived from 1,3-bis(3-aminopropyl)tetramethyldisiloxane and 3,5-di-tert-butyl-2-hydroxybenzaldehyde was prepared. The main feature of note is the 12-membered chelate ring formed upon coordination of the Schiff base to central atom, which adopts a distorted N₂O₄ octahedron environment. In the second step, the acetato co-ligand in this complex is replaced by the carboxylate anion of a dicarboxilic acid, namely adipic acid. This metathesis reaction leads to the formation of dinuclear structure by connecting two manganese centers. The structure, as was determined by X-ray single crystal diffractometry, elemental and spectral analysis, is permethylated dinuclear complex with long aliphatic bridge. Thermal and magnetic properties were studied. In addition, the formation of magnetically induced stripe-ordered domains was highlighted by the magnetic force microscopy (MFM) on films born from diluted solution.     

Three Reactions,One Catalyst: A Multi-Purpose Platinum(IV) Complex and its Silica-Supported Homologue for Environmentally Friendly Processes

Although platinum nanoparticles and complexes -especially of Pt(0) and Pt(II)- are well known catalysts, siloxane-based platinum complexes are rarely reported. Herein, a Platinum(IV) complex of 4-aminopyridinium-modified disiloxane was prepared and characterized by medium and far infrared spectroscopy, NMR and EDX. The formation of the complex was monitored by UV–Vis spectroscopy, which showed the high affinity and selectivity of this ligand for Pt, with a stability constant of 7.53·10³ M⁻¹. The catalytic activity of the siloxane-based complex was tested in three types of reactions: reduction of p-nitrophenol, oxidation of glucose and starch, and hydrosilylation. The hydrophobic behavior of the permethylated disiloxane moiety ensures good hydrolytic stability, while the N-donor ligand stabilizes the in-situ formed Pt nanoparticles. The generation of Pt nanoparticles during p-nitrophenol reduction was confirmed by TEM and SEM. Contrary to most reports, the aerobic oxidation of mono- and polysaccharides occurred without oxidation agents or mediators added, in mild conditions, at room temperature and pH ~9. The same metal complex was found active in hydrosilylation of vinyl-siloxanes with temperature-modulated rate, thus being useful in silicone cross-linking systems without the need of inhibitors. The method was adapted to one-pot synthesis of silica-supported Pt(IV) complex, which acted as efficient and reusable heterogeneous hydrosilylation catalyst, limiting the contamination of the product with Pt. This approach is promising for superior valorization of scarcely available and expensive platinum metal. By the same method, multifunctional soluble complexes and mesoporous silica may be obtained, with tunable catalytic performance.