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The crucial role of a protein corona in determining the aggregation kinetics and colloidal stability of polystyrene nanoplastics
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Time-resolved dynamic light scattering was used to study how protein coronas — protein layers that form on nanoplastics in biological or environmental fluids — control the aggregation kinetics and colloidal stability of polystyrene nanoplastics. Protein identity and concentration profoundly shifted nanoplastic behavior, with implications for how these particles move and persist in natural water systems.
Nanosized plastics are considered as being a class of contaminants of emerging concern. The interaction between nanoplastics and proteins may significantly influence the environmental behavior and fate of nanoplastics. Here, we employed time-resolved dynamic light scattering to explore the aggregation kinetics and stability of polystyrene nanoparticles (PSNPs) exposed to a model globular protein (bovine serum albumin, BSA) in the presence of a number of typical electrolytes (NaCl, CaCl, and NaSO). With the increase of the BSA concentration, the amount of BSA adsorbed on the surface of negatively charged PS-Bare (non-modified) and PS-COOH (carboxyl-modified) increased, resulting in higher dispersibility in comparison to the treatment without BSA. This stabilization effect derived from the protein corona structure was revealed by combining characterization techniques and visualized by transmission electron microscopy. Upon addition of NaCl and CaCl, the aggregation of positively charged PS-NH (amino-modified) was inhibited by the BSA addition possibly due to the screening of the attractive patch-charge force and the competition for adsorption of cations between PS-NH and the protein. When NaSO was present in the suspension, BSA addition significantly increased PS-NH aggregation rate due to patch-charge attraction and the high performance of SO in attaching to particles and charge neutralization. These findings shed light on the interactions between PSNPs and proteins, which were shown to vary with the composition of the surface coatings of PSNPs. The newly gained knowledge will help us to forecast the transport and fate of PSNPs in natural aqueous systems.
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Raman spectra characterization of size-dependent aggregation and dispersion of polystyrene particles in aquatic environments.
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This study used Raman spectroscopy to examine how the presence of salt, proteins, and organic matter influences the aggregation and dispersion of polystyrene nanoplastics in water. The findings show that environmental conditions significantly alter nanoplastic behavior and can complicate their detection, which has implications for understanding how nanoplastics move through aquatic environments.
Protein corona-induced aggregation of differently sized nanoplastics: impacts of protein type and concentration
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The aggregation behavior of two sizes of nanoplastic particles in aquatic environments differed depending on the electrical characteristics and concentration of proteins present. Protein coronas altered particle-particle interactions, with implications for nanoplastic fate and transport in natural water systems.
Aggregation behavior of polystyrene nanoplastics: Role of surface functional groups and protein and electrolyte variation
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Researchers studied how different surface coatings on polystyrene nanoplastics affect their tendency to clump together in water containing proteins and salts. They found that the type of surface functional group significantly changed how the particles aggregated, with proteins and electrolytes playing important roles in the process. The study helps explain how nanoplastics behave and transform as they move through natural water systems.
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