Binding of Tetrabromobisphenol A and S to Human Serum Albumin Is Weakened by Coexisting Nanoplastics and Environmental Kosmotropes

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, Delta Dh = 135 nm) and S (TBBPS, Delta Dh = 256 nm) at pH 7. At pH 4, these aggregates became larger with fewer electrostatic repulsion effects (Delta Dh = 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.

Automated summary

This study investigated the effects of brominated flame retardant (BFR) binding and corona formation on polystyrene nanoplastics (PNs) using human serum albumin (HSA) as a model protein. HSA helped disperse PNs under physiological conditions but promoted aggregate formation in the presence of tetrabromobisphenol A (TBBPA) and S (TBBPS). The aggregates became larger and had fewer electrostatic repulsion effects at pH 4. The effects of HSA and BFR binding varied due to structural differences of TBBPA and TBBPS.