18 research outputs found

    Dataset OROV

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    <p><b>First outbreak of Oropouche Fever reported in a non-endemic central-western region of the Peruvian Amazon. </b><b>Molecular diagnosis and clinical characteristics. </b></p><p><b>Introduction: </b>Oropouche virus (OROV) is an underreported and emerging infectious disease. Its incidence is underestimated mainly due to clinical similarities with other diseases that are also caused by arboviruses present in endemic areas. We report the first outbreak of OROV in the western region of the Peruvian Amazon in the department of Huanuco, Peru. </p><p><b>Methods</b>: This outbreak occurred in the region of Huanuco, Peru during July of 2016. Blood samples were taken from 268 patients who presented acute febrile syndrome to be later analyzed for Oropouche Virus via Polymerase Chain Reaction.</p><p><b>Results</b>: Of all 268 patients, 46 (17%) cases tested were positive for OROV. the most common symptom reported was headaches with a frequency of 87% (n=40) followed by myalgias with 76% (n=35), arthralgias with 65.2% (n=30), retro-ocular pain 60.8% (n=28) and hyporexia with 50% (n=23). </p><p> Concerning signs and symptoms that may suggest severe OROV infection, 4.3% (n=2) had low platelet count, 8.6% (n=4) had intense abdominal pain, and only 2.1% (n=1) had a presentation with thoracic pain<br></p

    Incorporation of a Clot-Binding Peptide into Polythiophene: Properties of Composites for Biomedical Applications

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    Biocomposites formed by a pentapeptide (CREKA), which recognizes clotted plasma proteins, entrapped into the poly­(3,4-ethylenedioxythiophene) (PEDOT) matrix have been prepared using three very different procedures. X-ray photoelectron spectroscopy analyses indicate that PEDOT-CREKA films, prepared by chronoamperometry in basic aqueous solution (pH = 10.3) and deposited onto a PEDOT internal layer, present the higher concentration of peptide: one CREKA molecule per six polymer repeat units. The surface of this bilayered system shows numerous folds homogeneously distributed, which have been exhaustively characterized by scanning electron microscopy and atomic force microscopy. Indeed, the morphology and topography of such bilayered films is completely different from those of biocomposite-prepared acid aqueous and organic solutions as polymerization media. The impact of the entrapped peptide molecules in the electrochemical properties of the conducting polymer has been found to be practically negligible. In contrast, biocompatibility assays with two different cellular lines indicate that PEDOT-CREKA favors cellular proliferation, which has been attributed to the binding of the peptide to the fibrin molecules from the serum used as a supplement in the culture medium. The latter assumption has been corroborated examining the ability of PEDOT-CREKA to bind fibrin. The latter ability has been also used to explore an alternative strategy based on the treatment of PEDOT-CREKA with fibrin to promote cell attachment and growth. Overall, the results suggest that PEDOT-CREKA is appropriated for multiple biomedical applications combining the electrochemical properties of conducting polymer and the ability of the peptide to recognize and bind proteins

    Polypyrrole-Supported Membrane Proteins for Bio-Inspired Ion Channels

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    Biomedical platforms constructed by immobilizing membrane proteins in matrixes made of synthetic organic polymers is a challenge because the structure and function of these proteins are affected by environmental conditions. In this work, an operative composite that regulates the diffusion of alkali ions has been prepared by functionalizing a supporting matrix made of poly­(<i>N</i>-methylpyrrole) (PNMPy) with a β-barrel membrane protein (Omp2a) that forms channels and pores. The protein has been unequivocally identified in the composite, and its structure has been shown to remain unaltered. The PNMPy–Omp2a platform fulfills properties typically associated with functional bio-interfaces with biomedical applications (e.g., biocompatibility, biodegrabadility, and hydrophilicity). The functionality of the immobilized protein has been examined by studying the passive ion transport response in the presence of electrolytic solutions with Na<sup>+</sup> and K<sup>+</sup> concentrations close to those found in blood. Although the behavior of PNMPy and PNMPy–Omp2a is very similar for solutions with very low concentration, the resistance of the latter decreases drastically when the concentration of ions increases to ∼100 mM. This reduction reflects an enhanced ion exchange between the biocomposite and the electrolytic medium, which is not observed in PNMPy, evidencing that PNMPy–Omp2a is particularly well suited to prepare bioinspired channels and smart biosensors

    Thermomechanical Response of a Representative Porin for Biomimetics

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    The thermomechanical response of Omp2a, a representative porin used for the fabrication of smart biomimetic nanomembranes, has been characterized using microcantilever technology and compared with standard proteins. For this purpose, thermally induced transitions involving the conversion of stable trimers to bigger aggregates, local reorganizations based on the strengthening or weakening of intermolecular interactions, and protein denaturation have been detected by the microcantilever resonance frequency and deflection as a function of the temperature. Measurements have been carried out on arrays of 8-microcantilevers functionalized with proteins (Omp2a, lysozyme and bovine serum albumin). To interpret the measured nanofeatures, the response of proteins to temperature has been also examined using other characterization techniques, including real time wide angle X-ray diffraction. Results not only demonstrate the complex behavior of porins, which exhibit multiple local thermal transitions before undergoing denaturation at temperatures higher than 105 °C, but also suggest a posttreatment to control the orientation of immobilized Omp2a molecules in functionalized biomimetic nanomembranes and, thus, increase their efficacy in ion transport
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