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Copper ferrite nanoparticles for use as MRI contrast agents were synthesized using two different methods. A novel microwave-assisted (MW) solvothermal method was developed and compared to a conventional 12-hour synthesis (Reflux) as an eco-friendlier approach. This innovative synthesis method successfully produced nanoparticles with enhanced properties compared to traditional ferrite materials. The nanoparticles' morphological and magnetic properties were evaluated and tested in in-vivo MRI studies. The results revealed both similarities and differences between the amine-functionalized copper ferrite nanoparticles. FTIR, XRD, HRTEM, and VSM analyses indicated improved properties in the CuFe2O4-NH2 MW particles, while AFM confirmed successful polymer encapsulation of the nanoparticles. For the CuFe2O4-NH2 MW sample, 76.8 wt% copper ferrite and 23.2 wt% magnetite were detected, with crystallite sizes of 8 ± 2 nm and 13 ± 2 nm, respectively. In the CuFe2O4-NH2 Refl. sample, in addition to these two magnetic phases, larger copper particles (31.6 wt%) were also formed. DLS analysis demonstrated that the CuFe2O4-NH2 MW sample exhibited excellent colloidal stability, maintaining its size distribution in aqueous media for 3 hours without aggregation, unlike the CuFe2O4-NH2 Refl. sample, which showed slight aggregation. The CuFe2O4-NH2 MW sample displayed superparamagnetic behavior (Ms: 15 emu/g, Mr: 0 emu/g, Hc: 0 Oe), while the CuFe2O4-NH2 Refl. sample exhibited ferromagnetic characteristics (Ms: 40 emu/g, Mr: 1.35 emu/g, Hc: 30 Oe). Both samples produced comparable results during in vitro MRI measurements, showing similar T2* relaxation and signal characteristics. Further in vivo studies demonstrated that both samples induced significant hypointense changes. The study provides valuable insights into the synthesis, properties, and potential applications of these materials, emphasizing the importance of eco-friendly methods and the optimization of ferrite-based MRI contrast agents. [ABSTRACT FROM AUTHOR]

Supercritical fluid chromatographic methods for enantiomer separation of six conazole-type antifungal pesticides (bromuconazole, cyproconazole, prothioconazole, tebuconazole, ipconazole, triticonazole) are presented in this work. Screening tests on six different chiral analytical columns (Chiralpak IA, Chiralpak IB, Chiralpak IC, Chiralpak AS, Chiracel OJ and Kromasil Cellucoat) were carried out using methanol as organic modifier. Cellulose-based stationary phases were found to be better for separation of each tested conazole, than the amylose-based columns. The influence of the most commonly used co-solvents (methanol, ethanol and 2-propanol) on the separation was also studied on selected columns. Suitable analytical methods were found for enantiomer separations for all studied conazoles; moreover, the methods are good starting points to semi-preparative separation. The importance of sample solvent selection in the semi-preparative separation of triticonazole isomers was proved. Acetonitrile as sample solvent resulted in a narrow, nice peaks compared to those obtained with methanol or dichloromethane. Twenty milligrams of each enantiomer of triticonazole was collected for ecotoxicity testing using the analytical size column. [ABSTRACT FROM AUTHOR]

Mass spectrometry has become the most prominent yet evolving technology in quantitative proteomics. Today, a number of label-free and label-based approaches are available for the relative and absolute quantification of proteins and peptides. However, the label-based methods rely solely on the employment of stable isotopes, which are expensive and often limited in availability. Here we propose a label-based quantification strategy, where the mass difference is identified by the differential alkylation of cysteines using iodoacetamide and acrylamide. The alkylation reactions were performed under identical experimental conditions; therefore, the method can be easily integrated into standard proteomic workflows. Using high-resolution mass spectrometry, the feasibility of this approach was assessed with a set of tryptic peptides of human serum albumin. Several critical questions, such as the efficiency of labeling and the effect of the differential alkylation on the peptide retention and fragmentation, were addressed. The concentration of the quality control samples calculated against the calibration curves were within the ±20% acceptance range. It was also demonstrated that heavy labeled peptides exhibit a similar extraction recovery and matrix effect to light ones. Consequently, the approach presented here may be a viable and cost-effective alternative of stable isotope labeling strategies for the quantification of cysteine-containing proteins. [ABSTRACT FROM AUTHOR]