Conjugated polymers nanostructured as smart interfaces for controlling the catalytic properties of enzymes
| Autor: | Luciano Caseli, Laura Oliveira Péres, Camila Gouveia Barbosa |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
Materials science
Polymers Surface Properties Infrared spectroscopy Thiophenes 02 engineering and technology Conjugated system 010402 general chemistry 01 natural sciences Langmuir–Blodgett film Fluorescence spectroscopy Biomaterials chemistry.chemical_compound Colloid and Surface Chemistry Monolayer Polymer chemistry Thiophene chemistry.chemical_classification Fluorine Polymer Enzymes Immobilized 021001 nanoscience & nanotechnology Urease Nanostructures 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials chemistry Chemical engineering Biocatalysis 0210 nano-technology Biosensor |
| Zdroj: | Journal of Colloid and Interface Science. 476:206-213 |
| ISSN: | 0021-9797 |
| Popis: | 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). Urease was incorporated in the floating monolayers being further transferred to solid supports as mixed Langmuir-Blodgett (LB) films. These films were then characterized with transfer ratio, fluorescence spectroscopy, PM-IRRAS and atomic force microscopy, confirming the co-transfer of the enzyme as well as its structuring in β-sheets. The catalytic activity was detected for urease, with a lower reaction rate than that encountered for the homogeneous environment. This was attributed to conformational constraints imposed to the biomacromolecule entrapped in the polymeric matrix. |
| Databáze: | OpenAIRE |
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