Neat and hybrid poly(2-pyrrolidone), i.e. polyamide 4 (PA4) microparticles containing magnetic or conductive metal, metal oxide, or carbon nanotube fillers were prepared via environmentally-friendly solventless activated ring-opening polymerization of 2-pyrrolidone at 40 C. The method produces high porosity microparticles with diameters of 5e12 mm and conversion to PA4 of 56e65%. Their structure and properties were characterized by light-and electron microscopy, thermal, spectral and Xray diffraction techniques. Two crystalline polymorphs, namely aÀ and bÀPА4, were found to coexist at room temperature by X-ray diffraction. The assessment of the adsorption capacity of the PA4 hybrid microparticles toward model protein showed up to 60% efficiency only after 1 h of incubation without any preliminary activation or functionalization.
This study reports on the synthesis and adsorption properties of molecularly imprinted porous magnetic microparticles (MIP) based on the biodegradable and sustainable poly(2-pyrrolidone) (PPD or PA4). These new PPD MIP materials were obtained via activated anionic ring-opening polymerization of 2-pyrroldone carried out at 40°C, in the presence of iron fillers and bovine serum albumin (BSA) as a template. Neither solvent, nor additional crosslinking or porogen agents were used in the PPD MIP synthesis. Analogously, PPD particles without BSA imprinting (NIP) were also produced. Depending on the microparticles composition, their yields were in the 55-70 wt% range, the average size varying between 8 and 25 µm. After characterization of the surface topography of all samples, their adsorption capacity toward the BSA target was assessed as a function of the adsorption time, protein concentration and pH of the medium. All three PPD MIP samples displayed adsorption capacity toward BSA being up to one order of magnitude higher as compared to other BSA-imprinted polymer systems. It was found that the rebinding of BSA on MIP is best described by the Langmuir isotherm, whereas for rebinding on NIP the Freundlich isotherm was the more adequate model. On this basis, the nature of the adsorption on MIP and NIP was discussed. The adsorption toward two other proteins, namely Ovalbumin and Cytochrome C was also tested. The newly synthesized BSA-imprinted PPD MIP displayed selective adsorption for the BSA target being dependent on the pH values of the medium. The easy recovery of the Fe-containing MIP and the capacity of all MIP samples for multiple sorption/desorption cycles was demonstrated.
Neat and hybrid polyamide 12 (PA12) based powders are important raw materials for additive manufacturing. This study describes a facile method for the synthesis of pure, hybrid and copolymeric microparticulate materials based on one‐pot activated anionic ring‐opening polymerization (AAROP) of laurolactam in solution. The results reveal the possibility to obtain in good yields, for reaction times of 2 h and temperatures of up to 110°C neat and hybrid PA12 microparticles (MP) carrying metal or carbon fillers. Copolymeric PA12/PA6 MP can also be successfully prepared. All MP materials are analyzed by spectral, microscopy, thermal, and synchrotron X‐ray scattering methods in order to clarify their morphology, chemical and crystalline structure, melting and degradation behavior. The melting temperature of the PA12 MP is lower than of the commercial PA12, the presence of metal particles or copolymerization with PA6 additionally decrease it well below 170°C. The composites prepared by compression molding of PA12 MP display elastic modulus of up to 1.49 GPa, the stresses at yield and break reaching 50 and 69 MPa, respectively. It is concluded that the neat, hybrid, and copolymeric pulverulent materials obtained via microencapsulation by AAROP in solution may be useful in additive manufacturing processing.
Herewith we report the first attempt towards non-covalent immobilization of Trametes versicolor laccase on neat and magnetically responsive highly porous polyamide 6 (PA6) microparticles and their application for catechol oxidation. Four polyamide supports, namely neat PA6 and such carrying Fe, phosphate-coated Fe and Fe3O4 cores were synthesized in suspension by activated anionic ring-opening polymerization (AAROP) of ε-caprolactam (ECL). Enzyme adsorption efficiency up to 92% was achieved in the immobilization process. All empty supports and PA6 laccase complexes were characterized by spectral and synchrotron WAXS/SAXS analyses. The activity of the immobilized laccase was evaluated using 2,2’-Azino-bis-(3- ethylbenzothiazoline-6-sulfonic acid (ABTS) and compared to the native enzyme. The PA6 laccase conjugates displayed up to 105% relative activity at room temperature, pH 4, 40 °C and 20 mM ionic strength (citrate buffer). The kinetic parameters of the ABTS oxidation were also determined. The reusability of the immobilized laccase-conjugates was proven for five consecutive oxidation cycles of catechol.
This work presents the preparation, optimization, and testing of an enzymebased optical biosensor for catechol determination. The sensing area is attached to a glass support and contains: anionic polyamide 6 (PA6) porous microparticles supporting laccase from Trametes Versicolor, embedded in a Pebax ® MH1657 polymer binder that contains the optical indicator dye 3-methyl-2-benzothiazolinone hydrazone (MBTH), responsible for the optical transduction. The catechol analyte, after its enzymatic oxidation, forms o-benzoquinone that can be detected by oxidative coupling with MBTH giving rise to a colored product. The latter can be quantified measuring the UV/VIS absorbance at 500 nm. The PA6 microparticles performed as useful laccase carriers reaching high immobilization yields of up to 99.8% and preserving the enzyme catalytic activity. This permitted the preparation of a new biosensor presenting a detection limit of 11 μM and responding linearly to up to 118 μM of catechol. Biosensor applicability was tested in spiked natural water samples from river and spring. The recovery rates observed were in the range of 97-108% that proves the good accuracy of the proposed biosensor.
Anti-EFG1 2′-OMethylRNA is an antisense oligonucleotide (ASO) that has the ability to recognize and block the EFG1 gene and to control Candida albicans filamentation. However, it is important to protect the anti-EFG1 2′-OMethylRNA ASO from the environmental human body conditions and to ensure that they will be delivered to their site of action, and polyplex microparticles (MPs) represent a class of vehicles to ASO cargo with these functionalities. Thus, the goal of this work was to develop polyplexes based on porous poly(γ-butyrolactam) (PA4) or poly(ε-caprolactam) (PA6) MPs for the anti-EFG1 2′-OMethylRNA ASO cargo and delivery. Two types of polyplexes were prepared with payloads of anti-EFG1 2′-OMethylRNA molecules, either entrapped or immobilized on prefabricated polyamide MPs. Our data confirm that PA4 and PA6 polyplex MPs can be feasible carriers for anti-EFG1 2′-OMethylRNA ASO molecules, using either the entrapment or immobilization strategies, whereby the released ASO maintains its activity against C. albicans cells.
This study reports on the synthesis of novel bienzyme polymer-assisted nanoflower complexes (PANF), their morphological and structural characterization, and their effectiveness as cascade biocatalysts. First, highly porous polyamide 6 microparticles (PA6 MP) are synthesized by activated anionic polymerization in solution. Second, the PA6 MP are used as carriers for hybrid bienzyme assemblies comprising glucose oxidase (GOx) and horseradish peroxidase (HRP). Thus, four PANF complexes with different co-localization and compartmentalization of the two enzymes are prepared. In samples NF GH/PA and NF GH@PA, both enzymes are localized within the same hybrid flowerlike organic-inorganic nanostructures (NF), the difference being in the way the PA6 MP are assembled with NF. In samples NF G/PAiH and NF G@PAiH, only GOx is located in the NF, while HRP is preliminary immobilized on PA6 MP. The morphology and the structure of the four PANF complexes have been studied by microscopy, spectroscopy, and synchrotron X-ray techniques. The catalytic activity of the four PANF was assessed by a two-step cascade reaction of glucose oxidation. The PANF complexes are up to 2–3 times more active than the free GOx/HRP dyad. They also display enhanced kinetic parameters, superior thermal stability in the 40–60 °C range, optimum performance at pH 4–6, and excellent storage stability. All PANF complexes are active for up to 6 consecutive operational cycles.
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