Publications by authors named "Laura Oliveira Peres"

Thin films of conjugated polymer and enzyme can be used to unravel the interaction between components in a biosensor. Using artificial neural networks (ANNs) improves data interpretability and helps construct models with great capacity for classifying and processing information. The present work used kinetic data from the catalytic activity of urease immobilized in different conjugated polymers to create ANN models using time, substrate concentration, and absorbance as input variables since the models had absorbance in a posterior instant as output value to explore the predictivity of the ANNs.

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The use of conjugated polymers (CPs) and metallic nanoparticles is an interesting way to form nanocomposites with improved optical properties. For instance, a nanocomposite with high sensitivity can be produced. However, the hydrophobicity of CPs may hamper applications due to their low bioavailability and low operability in aqueous media.

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In this study, we report on crystallographic studies that were performed on Na- and K-doped terphenyl and quaterphenyl. The data obtained via X-ray scattering and transmission electron diffraction show that, for both K-doped terphenyl and quaterphenyl samples, there is an increase in the parameter. However, in regard to Na-doped terphenyl, there is a parameter decrease along with an parameter increase, which may be accounted for by the polymerization of this oligomer.

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Initially developed for classic systems composed of fatty acids and phospholipids, the Langmuir and Langmuir-Blodgett (LB) techniques allow the fabrication of nanometer-scale devices at self-assembly interfaces with high control over the thickness and molecular architecture. Their application in the research and production of new plastic materials has grown considerably over the past few decades due to the efficiency of conjugated polymers (CPs) for the production of light-emitting diodes, flexible displays, solar cells, and other photoelectronic devices. The structuring of polymers at different interfaces is not trivial as this class of macromolecules can undergo through different processes of folding/unfolding, which hinders the formation of stable Langmuir monolayers and, consequently, the production of Langmuir-Blodgett films.

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In this work, the copolymer poly[(9,9-dioctylfluorene)--(3-hexylthiophene)] was employed as a matrix for immobilizing phytase, aiming at the detection of phytic acid. The copolymer was spread on the air-water interface forming Langmuir monolayers and phytase adsorbed from the aqueous subphase. The interactions between the copolymer and the enzyme components were investigated with surface pressure and surface potential-area isotherms, Brewster angle microscopy, and polarization modulation infrared reflection-absorption spectroscopy (PM-IRRAS).

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The structure of enzymes must be conserved when incorporated in nanoelectronic devices because their activity determines the function of the device as sensors. Among the systems that can retain their conformational structures, Langmuir-Blodgett (LB) films can be useful to exploit the construction of bioelectronic devices organized at the molecular level because biological and polymeric materials can be coupled as ultrathin films for biosensors and actuators. In this paper, we immobilized a β-galactosidase enzyme in the LB films of stearic acid and the conjugated polymer poly[(9,9-dioctylfluorene)- co-thiophene].

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The search for new molecular architectures to improve the efficiency of enzymes entrapped in ultrathin films is useful to enhance the effectiveness of biosensors. In this present work, conjugated polymers, based on thiophene and fluorine, were investigated to verify their suitability as matrices for the immobilization of urease. The copolymer poly[(9,9-dioctylfluorene)-co-thiophene], PDOF-co-Th was spread on the air-water interface forming stable Langmuir monolayers as determined by surface pressure-area isotherms, polarization-modulation reflection-absorption infrared spectroscopy (PM-IRRAS), and Brewster angle microscopy (BAM).

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