Over the past few years, superparamagnetic iron oxide nanoparticles (SPIONs) have attracted much attention due to their medicinally attractive properties and their possible application in cancer diagnosis and therapy. However, there is still a lack of appropriate methods to enable quantitative monitoring of the particle changes in a physiological environment, which could be beneficial for evaluating their in vitro and in vivo behavior. For this reason, the main goal of this study was the development of a novel capillary electrophoresis-inductively coupled plasma mass spectrometry (CE-ICP-MS/MS) method for the determination of SPIONs suitable for the future examination of their changes upon incubation with proteins under simulated physiological conditions. The type and flow rate of the collision/reaction gas were chosen with the aim of simultaneous monitoring of Fe and S. The type and concentration of the background electrolyte, applied voltage, and sample loading were optimized to obtain SPION signals of the highest intensity and minimum half-width of the peak. Analytical parameters were at a satisfactory level: reproducibility (intra- and inter-day) of migration times and peak areas (presented as RSD) in the range of 0.23–4.98%, recovery: 96.7% and 93.3%, the limit of detection (for monitoring 56Fe16O+ by mass-shift approach) 54 ng mL−1 Fe (0.97 μM) and 101 ng mL−1 Fe (1.82 μM) for SPIONs with carboxyl and amino terminal groups, respectively. To the best of our knowledge, this is the first reported use of CE-ICP-MS/MS for the quantification of SPIONs and monitoring of interactions with proteins.
Progress toward translating superparamagnetic iron oxide nanoparticles (SPIONs) with specific diagnostic and therapeutic properties for clinical applications depends on developing and implementing appropriate methodologies that would allow in-depth characterizations of their behavior in a real biological environment. Herein, we report a versatile approach for studying interactions between SPIONs and proteins using single-particle inductively coupled plasma tandem mass spectrometry. By monitoring the changes in the size distribution upon exposure to human serum, the formation of stable protein corona is revealed, accompanied by particle disaggregation.
Simple ultraviolet–visible spectroscopy-based methodology was proposed and utilized for the initial characterization of potential changes in selectivity of doped magnetic nanoparticles. Doped and undoped iron(II,III) (Fe3O4) magnetic nanoparticles were synthesized by the coprecipitation method. The doping processes of nanoparticles were confirmed using optical emission spectrometry, while the sizes of undoped and Cu-doped nanoparticles were investigated using a high-resolution field emission scanning electron microscope. The average diameters of nanoparticles were 8.34±1.78 nm and 9.12±1.93 nm, for doped and undoped materials, respectively. The influence of the nanoparticle's doping on their selectivity towards chosen analyte was monitored by the spectral techniques such as ultraviolet–visible and optical emission spectrometry. The interaction between Cu-doped Fe3O4 nanoparticles and cuprizone (a compound forming the characteristic colorful complex with copper) was confirmed. The elaborated studies proved the potential of ultraviolet–visible spectroscopy for the fast qualification of magnetic nanoparticles in terms of their ability to separate the selected analyte from the sample matrix.
The growing interest in superparamagnetic iron oxide nanoparticles (SPIONs) as potential theranostic agents is related to their unique properties and the broad range of possibilities for their surface functionalization. However, despite the rapidly expanding list of novel SPIONs with potential biomedical applications, there is still a lack of methodologies that would allow in-depth investigation of the interactions of those nanoparticles with biological compounds in human serum. Herein, we present attempts to employ capillary electrophoresis-inductively coupled plasma tandem mass spectrometry (CE-ICP-MS/MS) for this purpose and various obstacles and limitations noticed during the research. The CE and ICP-MS/MS parameters were optimized, and the developed method was used to study the interactions of two different proteins (albumin and transferrin) with various synthesized SPIONs. While the satisfactory resolution between proteins was obtained and the method was applied to examine individual reagents, it was revealed that the conjugates formed during the incubation of the proteins with SPIONs were not stable under the conditions of electrophoretic separation.
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