102 research outputs found

    Photothermal Study of Two Different Nanofluids Containing SiO2 and TiO2 Semiconductor Nanoparticles

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    Thermal and optical properties of two different nanofluids containing SiO2 and TiO2 semiconductor nanoparticles were studied by thermal lens spectrometry (TLS) and spectrophotometry. In the case of SiO2 nanofluids the transmission electron microscopy technique was used to obtain the SiO2 nanoparticle sizes to investigate the size effect of these nanoparticles on the sample thermal diffusivity which is important in some medical applications such as photothermal-modulated drug delivery systems. on the other hand for the case of TiO2 nanofluids, the photopyroelectric technique, TLS, scanning electron microscopy, and X-ray diffraction were employed to investigate the concentration effect on the thermal properties of these nanofluids. Thermal diffusivities and effusivities as functions of the TiO2 nanoparticle concentrations were obtained. From the experimental results, an incremental increase in the thermal diffusivities and effusivities was observed when the nanoparticle concentration was increased, indicating that the nanoparticle concentration is an important factor to be considered to obtain nanofluids with more thermal efficiency which are required for some applications, such as degradation of residual water.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES

    Functional Interactions of Human Immunodeficiency Virus Type 1 Integrase with Human and Yeast HSP60

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    Integration of human immunodeficiency virus type 1 (HIV-1) proviral DNA in the nuclear genome is catalyzed by the retroviral integrase (IN). In addition to IN, viral and cellular proteins associated in the high-molecular-weight preintegration complex have been suggested to be involved in this process. In an attempt to define host factors interacting with IN, we used an in vitro system to identify cellular proteins in interaction with HIV-1 IN. The yeast Saccharomyces cerevisiae was chosen since (i) its complete sequence has been established and the primary structure of all the putative proteins from this eucaryote has been deduced, (ii) there is a significant degree of homology between human and yeast proteins, and (iii) we have previously shown that the expression of HIV-1 IN in yeast induces a lethal phenotype. Strong evidences suggest that this lethality is linked to IN activity in infected human cells where integration requires the cleavage of genomic DNA. Using IN-affinity chromatography we identified four yeast proteins interacting with HIV-1 IN, including the yeast chaperonin yHSP60, which is the counterpart of human hHSP60. Yeast lethality induced by HIV-1 IN was abolished when a mutated HSP60 was coexpressed, therefore suggesting that both proteins interact in vivo. Besides interacting with HIV-1 IN, the hHSP60 was able to stimulate the in vitro processing and joining activities of IN and protected this enzyme from thermal denaturation. In addition, the functional human HSP60-HSP10 complex in the presence of ATP was able to recognize the HIV-1 IN as a substrate
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