RESUMEN

The electron absorption and emission spectra were measured for the pyramidal LnPc(OAc) complexes in the solid state and co-doped in silica glass, where Ln=Er, Eu and Ho. The theoretical electron spectra were determined from the quantum chemical DFT calculation using four approximations CAM-B3LYP/LANL2DZ, CAM-B3LYP/CC-PVDZ, B3LYP/LANL2DZ and B3LYP/CC-PVDZ. It was shown that the best agreement between the calculated and experimental structural parameters and spectroscopic data was reached for the CAM-B3LYP/LANL2DZ model. The emission spectra were measured using the excitations both in the ligand and lanthanide absorption ranges. The possibility of energy transfer between the phthalocyanine ligand and excited states of lanthanide ions was discussed. It was shown that the back energy transfer from metal states to phthalocyanine state is responsible for the observed emission of the studied complexes both in the polycrystalline state and silica glass.

RESUMEN

We report the synthesis, crystal structure, IR, Raman and luminescence studies of four metal-organic frameworks of the following formulas: [CH3CH2NH3]Y1-x-yYbyErx(HCOO)4 (x = 1, y = 0; x = 0.2, y = 0.8; x = 0.02, y = 0.07) and [CH3CH2NH3]Y0.92Eu0.08(HCOO)4. All the compounds are isostructural and crystallize in a polar and non-centrosymmetric monoclinic system (P21 space group). They have been characterized by single crystal and powder X-ray diffraction methods as well as by vibrational spectroscopy (IR and Raman). The assignment of the external and internal modes has been discussed and presented. Furthermore, the optical properties of the Er3+ and Eu3+ ions have been assessed using diffuse absorption, excitation and emission spectra. The site symmetry of the Eu3+ ions has been analyzed using the emission spectrum and the luminescence decay of the red emission.

RESUMEN

Undoped and Ag-doped TiO2 ceramics have been prepared at temperatures between 500-1000 °C and under pressures up to 8 GPa. Their crystal structures and physical properties were investigated by means of EDX, SEM, TEM, X-ray powder diffraction, and magnetization M, specific heat Cp and electrical resistance ρ measurements. It is found that the anatase-structured As-cast powder transforms into rutile and columbite-type at 500 °C and 5.5 GPa. The stabilization of the latter phase is fulfilled under a pressure of 8 GPa and at temperatures above 800 °C. On the basis of experimental results, we conclude that the physical properties of TiO2 can be tailored along with its crystal structure. In particular, magnetic properties change from paramagnetic in anatase and rutile to magnetic correlations and in all likelihood magnetic-field-induced antiferromagnetic short-range order in columbite-structured TiO2. Contrasting behaviour in the temperature dependences of specific heat between anatase/rutile and columbite-type TiO2 is obvious. Differently from anatase/rutile, the Cp of columbite-type TiO2 exhibits a low-temperature excess, being interpreted as due to magnetic correlations, or else the prevalence of soft modes. An analysis of ρ(T) for columbite-type TiO2 in the temperature range of 280-400 K reveals the presence of a new trapping state at an energy level of ∼28 meV within the originally forbidden gap. Furthermore, thermal fluctuation-induced tunnelling and hopping conductivities are suggested to govern in a lower temperature range. We recognize that the Ag-doped contents do not alter the crystal structure but considerably enhance magnetic correlations, compared to undoped samples.

RESUMEN

A new conjugate material based on partially reduced graphite oxide (rGO), silver nanoparticles (Ag), and bis(lysinato)zirconium(IV) phthalocyanine complex (ZrPc) was obtained. Its optical properties (absorption and photoluminescence) after dispersion in solvents were examined. The antimicrobial properties were tested to determine the effect of the composite on the following bacterial strains: Staphylococcus aureus, Pseudomonas aeruginosa, and Escherichia coli, which are responsible for many infections and are one of the pathogens the most difficult to treatment. The results obtained for rGO-ZrPc-Ag composite were compared with the properties of GO, GO-ZrPc, and rGO-Ag structures. The influence of the near-infrared irradiation on the antimicrobial activity of ZrPc- and Ag-doped materials against bacteria was observed for very low concentration (0.32mg/mL) of GO-ZrPc to stop the growth of P. aeruginosa in comparison to the nonirradiated sample (41mg/mL). The usefulness of this material in therapy, such as wound infection treatment or endodontic treatment, as antibacterial agent with sustained action was discussed.

Asunto(s)

Antiinfecciosos , Bacterias/crecimiento & desarrollo , Grafito , Rayos Infrarrojos , Nanopartículas del Metal/química , Plata/química , Antiinfecciosos/síntesis química , Antiinfecciosos/química , Antiinfecciosos/farmacología , Preparaciones de Acción Retardada/síntesis química , Preparaciones de Acción Retardada/química , Preparaciones de Acción Retardada/farmacología , Grafito/química , Grafito/farmacología , Humanos

RESUMEN

An efficient anti-Stokes white broadband emission induced by 976 nm laser diode in lithium ytterbium tetraphosphate (LiYbP4O12) nanocrystals was investigated. The emission occurs at room temperature and atmospheric pressure. Its intensity demonstrates an evident threshold dependence on the temperature and excitation density characteristic to avalanche process. The white emission is accompanied by very efficient photoconductivity characterized by microampere photocurrent which increases with the fourth order of applied incident light power (~P4). We show that this emission is critically dependent on temperature and increases significantly in vacuum. It is concluded that the anti-Stokes white emission is associated with theYb3+- CT luminescence.

RESUMEN

A wet chemical approach was employed for the preparation of LiEu(PO(3))(4) nanoparticles. XRD, Raman spectroscopy, TEM, SAED, and IR measurements were used in order to determine the crystal structure and morphology of the obtained product. Complete optical studies including absorption, excitation, emission, and kinetic measurements were performed. At least two components of the (5)D(0) → (7)F(0) transition were found, indicating the existence of more than one crystallographic position of the Eu(3+) ions. Asymmetry parameter R as well as the covalence of the Eu-O bond were found to decrease with the grain growth.

RESUMEN

Telomerase RNA is an essential component of the ribonucleoprotein enzyme involved in telomere length maintenance, a process implicated in cellular senescence and cancer. Vertebrate telomerase RNAs contain a box H/ACA snoRNA motif that is not required for telomerase activity in vitro but is essential in vivo. Using the Xenopus oocyte system, we have found that the box H/ACA motif functions in the subcellular localization of telomerase RNA. We have characterized the transport and biogenesis of telomerase RNA by injecting labeled wild-type and variant RNAs into Xenopus oocytes and assaying nucleocytoplasmic distribution, intranuclear localization, modification, and protein binding. Although yeast telomerase RNA shares characteristics of spliceosomal snRNAs, we show that human telomerase RNA is not associated with Sm proteins or efficiently imported into the nucleus. In contrast, the transport properties of vertebrate telomerase RNA resemble those of snoRNAs; telomerase RNA is retained in the nucleus and targeted to nucleoli. Furthermore, both nuclear retention and nucleolar localization depend on the box H/ACA motif. Our findings suggest that the H/ACA motif confers functional localization of vertebrate telomerase RNAs to the nucleus, the compartment where telomeres are synthesized. We have also found that telomerase RNA localizes to Cajal bodies, intranuclear structures where it is thought that assembly of various cellular RNPs takes place. Our results identify the Cajal body as a potential site of telomerase RNP biogenesis.

Asunto(s)

Núcleo Celular/metabolismo , ARN Nucleolar Pequeño/metabolismo , ARN/metabolismo , Telomerasa/metabolismo , Transporte Activo de Núcleo Celular , Animales , Compartimento Celular , Nucléolo Celular/metabolismo , Cuerpos Enrollados/metabolismo , Humanos , Modelos Moleculares , Conformación de Ácido Nucleico , Xenopus

RESUMEN

U3 small nucleolar RNA (snoRNA) is a member of the Box C/D family of snoRNAs which functions in ribosomal RNA processing. U3-55k is a protein that has been found to interact with U3 but not other members of the Box C/D snoRNA family. We have found that interaction of the U3-55k protein with U3 RNA in vivo is mediated by the conserved Box B/C motif which is unique to U3 snoRNA. Mutation of Box B and Box C, but not of other conserved sequence elements, disrupted interaction of U3-55k with U3 RNA. Furthermore, a fragment of U3 containing only these two conserved elements was bound by U3-55k in vivo. RNA binding assays performed in vitro indicate that Box C may be the primary determinant of the interaction. We have cloned the cDNA encoding the Xenopus laevis U3-55k protein and find strong homology to the human sequence, including six WD repeats. Deletion of WD repeats or sequences near the C-terminus of U3-55k resulted in loss of association with U3 RNA and also loss of localization of U3-55k to the nucleolus, suggesting that protein-protein interactions contribute to the localization and RNA binding of U3-55k in vivo.

Asunto(s)

ARN Nucleolar Pequeño/metabolismo , Ribonucleoproteínas Nucleolares Pequeñas/metabolismo , Secuencias de Aminoácidos , Secuencia de Aminoácidos , Animales , Clonación Molecular , Humanos , Datos de Secuencia Molecular , Unión Proteica , ARN Nucleolar Pequeño/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Secuencias Repetitivas de Ácidos Nucleicos , Ribonucleoproteínas Nucleolares Pequeñas/química , Homología de Secuencia de Aminoácido , Xenopus laevis

RESUMEN

The two major families of small nucleolar RNAs (snoRNAs), Box C/D and Box H/ACA, are generated in the nucleoplasm and transported to the nucleolus where they function in rRNA processing and modification. We have investigated the sequences involved in the intranuclear transport of Box H/ACA snoRNAs by assaying the localization of injected fluorescent RNAs in Xenopus oocyte nuclear spreads. Our analysis of U17, U64 and U65 has revealed that disruption of either of the conserved sequence elements, Box H or Box ACA, eliminates nucleolar localization. In addition, the stem present at the base of the 3' hairpin is required for efficient nucleolar localization of U65. Fragments or rearrangements of U65 that consist of Box H and Box ACA flanking either the 5' or 3' hairpin are targeted to the nucleolus. The targeting is dependent on the presence of the Box sequences, but not on their orientation. Our results indicate that in each of the two major families of snoRNAs, a motif composed of the signature conserved sequences and an adjacent structural element that tethers the sequence elements directs the nucleolar localization of the RNAs. We demonstrate that telomerase RNA is also targeted to the nucleolus by a Box ACA-dependent mechanism.

Asunto(s)

ARN Nucleolar Pequeño/genética , ARN Nucleolar Pequeño/metabolismo , Animales , Secuencia de Bases , Nucléolo Celular/metabolismo , Secuencia Conservada , Femenino , Humanos , Técnicas In Vitro , Datos de Secuencia Molecular , Mutación , Señales de Localización Nuclear/genética , Conformación de Ácido Nucleico , Oocitos/metabolismo , ARN Nucleolar Pequeño/química , Telomerasa/genética , Xenopus

RESUMEN

Activated forms of Bacillus thuringiensis insecticidal toxins have consistently been found to form insoluble and inactive precipitates when they are expressed in Escherichia coli. Genetic engineering of these proteins to improve their effectiveness as biological pesticides would be greatly facilitated by the ability to express them in E. coli, since the molecular biology tools available for Bacillus are limited. To this end, we show that activated B. thuringiensis toxin (Cry1Ac) can be expressed in E. coli as a translational fusion with the minor phage coat protein of filamentous phage. Phage particles displaying this fusion protein were viable, infectious, and as lethal as pure toxin on a molar basis when the phage particles were fed to insects susceptible to native Cry1Ac. Enzyme-linked immunosorbent assay and Western blot analysis showed the fusion protein to be antigenically equivalent to native toxin, and micropanning with anti-Cry1Ac antibody was positive for the toxin-expressing phage. Phage display of B. thuringiensis toxins has many advantages over previous expression systems for these proteins and should make it possible to construct large libraries of toxin variants for screening or biopanning.

Asunto(s)

Fagos de Bacillus/genética , Bacillus thuringiensis/genética , Proteínas Bacterianas/genética , Proteínas Bacterianas/toxicidad , Toxinas Bacterianas , Endotoxinas/genética , Endotoxinas/toxicidad , Insecticidas , Biblioteca de Péptidos , Secuencia de Aminoácidos , Animales , Toxinas de Bacillus thuringiensis , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo , Bacteriófago lambda/genética , Endotoxinas/química , Endotoxinas/metabolismo , Ensayo de Inmunoadsorción Enzimática , Escherichia coli/genética , Escherichia coli/metabolismo , Ingeniería Genética , Vectores Genéticos , Proteínas Hemolisinas , Immunoblotting , Datos de Secuencia Molecular , Proteínas Recombinantes de Fusión/química , Proteínas Recombinantes de Fusión/metabolismo , Proteínas Recombinantes de Fusión/toxicidad