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Phosphate ions perform a variety of functions in metabolic processes and are essential for all living organisms. The determination of the concentration of phosphate ions is useful in clinical diagnosis of various diseases as an inadequate phosphate level could lead to many health problems. In the search for a cost-effective method of fast monitoring, we investigated the use of cobalt ferrite nanoparticles (CoFeNPs) in the selective recognition of phosphate ions dissolved in aqueous media and more complex samples, such as human blood serum. We prepared these NPs by a chemical coprecipitation route and subjected them to annealing at 600 °C for 1 h. The successful formation of the NPs was confirmed by Fourier transform infrared spectroscopy, X-ray diffraction, transmission electron microscopy, and hysteresis loop measurements. The NPs exhibited a ferrimagnetic behavior, a spineltype crystalline structure, and hexagonal shape in the nanoscale range. We demonstrated that CoFeNPs containing immobilized fluorescent-labeled single-chain DNA (ssDNA*) probes can be applied for the fast selective detection of phosphate ions dissolved in a liquid medium. We have explored the fact that phosphate groups can displace ssDNA* probes attached to the nanoparticles, therefore causing a perceptible change in the fluorescence signal of the supernatant liquid. This detection method has been tested for the sensing of phosphate ions present both in aqueous solutions and in biological samples, with excellent selectivity and a low limit of detection (∼1.75 nM).

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This paper reports on the study of the interactions between ascorbic acid (AA) and bovine serum albumin (BSA) in aqueous solution as well as in films (BSA/AA films) prepared by the layer-by-layer technique. Regarding to solution studies, a hyperchromism (in the range of ultraviolet) was found as a function of AA concentration, which suggested the formation of aggregates from AA and BSA. Binding constant, K, determined for aggregates from BSA and AA was found to be about 102 M−1, which indicated low affinity of AA with BSA. For the BSA/AA films, it was also noted that the AA adsorption process and surface morphological structures depended on AA concentration. By changing the contact time between the AA and BSA, a hypochromism was revealed, which was associated to decrease of accessibility of solvent to tryptophan due to formation of aggregates. Furthermore, different morphological structures of aggregates were observed, which were attributed to the diffusion-limited aggregation. Since most of studies of interactions of drugs and proteins are performed in solution, the analysis of these processes by using films can be very valuable because this kind of system is able to employ several techniques of investigation in solid state.