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Differential aggregation of polystyrene and titanium dioxide nanoparticles under various salinity conditions and against multiple proteins types
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Researchers compared the aggregation behavior of polystyrene and titanium dioxide nanoparticles under varying salinity conditions and with different protein types, finding that increasing salinity destabilized both nanoparticle types but had a stronger effect on polystyrene. Bovine serum albumin formed a protein corona that modified colloidal stability in a time-dependent manner.
The interaction of nanoplastics (NPls) and engineered nanoparticles (ENPs) with organic matter and environmental pollutants is particularly important. Therefore, their behavior should be investigated under the different salinity conditions, mimicking rivers and coastal environments, to understand this phenomenon in those areas. In this work, we analyzed the elementary characteristics of polystyrene-PS (unmodified surface and modified with amino or carboxyl groups) and titanium dioxide-TiO2 nanoparticles. The effect of salinity on their colloidal properties was studied too. Also, the interaction with different types of proteins (bovine serum albumin-BSA and tilapia proteins), as well as the formation of the BSA corona and its effect on the colloidal stability of nanoparticles, were evaluated. The morphology and dispersion of sizes were more uniform in unmodified-surface PS-NPs (70.5 ± 13.7 nm) than in TiO2-NPs (131.2 ± 125.6 nm). Likewise, Rama spectroscopy allowed recognizing peaks associated with the PS phenyl group aromatic ring in unmodified-surface PS-NPs (621, 1002, 1582, and 1602 cm). For TiO2-NPs, the data suggest belonging to the tetragonal form, also known as rutile (445, 610 cm). The elevation of salinity dose-dependently decreased NP colloid stability, with more significant variation in the PS-NPs compared to TiO2-NPs. The organic matter is also involved in this phenomenon, differentially as a function of time compared to its absence (unmodified-surface PS-NPs 30 psu/TOC 5 mgL/24 h: 2876.6 ± 378.03 nm; unmodified-surface PS-NPs 30 psu/24 h: 2133 ± 49.57 nm). In general, the TiO2-NPs demonstrated greater affinity with all proteins tested (0.066 g/L). It was observed that morphology, size, and surface chemical modification intervene in a relevant way in the interaction of the nanoparticles with bovine serum albumin (unmodified-surface PS-NPs 298 K: 6.08E; 310 K: 6.63E; TiO2-NPs 298 K: 8.76E; 310 K: 1.05E L mol) and tilapia tissues proteins (from blood, gills, liver, and brain). Their morphology and size also determined the protein corona formation and the NPs' agglomeration. These findings can provide references during knowledge transfer between NPls and ENPs.
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