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Binding of Tetrabromobisphenol A and S to Human Serum Albumin Is Weakened by Coexisting Nanoplastics and Environmental Kosmotropes
Summary
Researchers studied how polystyrene nanoplastics interact with human serum albumin and brominated flame retardants (TBBPA and TBBPS) under various conditions. The study found that while the protein helped disperse nanoplastics alone, adding flame retardants promoted aggregate formation, with environmental salt conditions further influencing these interactions. These findings suggest that the behavior of nanoplastics and co-occurring pollutants in both biological and natural water systems may be more complex than previously understood.
Human serum albumin (HSA) was used as a model protein to explore the effects of brominated flame retardant (BFR) binding and the corona formation on polystyrene nanoplastics (PNs). Under physiological conditions, HSA helped to disperse PNs but promoted the formation of aggregates in the presence of tetrabromobisphenol A (TBBPA, ΔDh = 135 nm) and S (TBBPS, ΔDh = 256 nm) at pH 7. At pH 4, these aggregates became larger with fewer electrostatic repulsion effects (ΔDh = 920 and 691 nm for TBBPA and TBBPS, respectively). However, such promotion effects as well as BFR binding are different due to structural differences of tetrabromobisphenol A and S. Environmental kosmotropes efficiently stabilized the structure of HSA and inhibited BFR binding, while the chaotropes favored bioconjugated aggregate formation. Such effects were also verified in natural seawater. The newly gained knowledge may help us anticipate the behavior and fate of plastic particles and small molecular pollutants in both physiological and natural aqueous systems.