We can't find the internet
Attempting to reconnect
Something went wrong!
Hang in there while we get back on track
Binding of Tetrabromobisphenol A and S to Human Serum Albumin Is Weakened by Coexisting Nanoplastics and Environmental Kosmotropes
AI summary Read the abstract
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.
More Papers Like This
Aggregation behavior of polystyrene nanoplastics: Role of surface functional groups and protein and electrolyte variation
AI summary Read the abstract
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.
Association of tetrabromobisphenol A (TBBPA) with micro/nano-plastics: A review of recent findings on ecotoxicological and health impacts
AI summary Read the abstract
This review examines how tetrabromobisphenol A (TBBPA), a widely used flame retardant found in plastic products, binds to micro and nanoplastics in the environment. When TBBPA hitches a ride on microplastics, the combined effect on organisms and ecosystems is often worse than either contaminant alone. Since TBBPA is an additive in many plastic products, the findings highlight how microplastics can carry harmful chemicals directly into the body.
Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin
AI summary Read the abstract
Scientists found that when nanoplastics and triclosan (an antimicrobial chemical) are present together, the nanoplastics make triclosan bind more strongly to human serum albumin, a key blood protein. This stronger binding disrupts the protein's normal enzyme function more than triclosan alone would. The findings are concerning because people are exposed to both nanoplastics and triclosan simultaneously, and their combined effect on blood proteins could be worse than either substance individually.
Influence of protein configuration on aggregation kinetics of nanoplastics in aquatic environment
AI summary Read the abstract
Researchers investigated how five different proteins with varying structures affect the aggregation behavior of polystyrene nanoplastics in water under different ionic strength and pH conditions. They found that protein type and configuration significantly influenced whether nanoplastics clumped together or remained dispersed, with globular proteins like albumin having different effects than fibrous proteins like collagen. The study suggests that the protein composition of natural waters plays an important role in determining how nanoplastics behave and transport in aquatic environments.
Influence of environmental and biological macromolecules on aggregation kinetics of nanoplastics in aquatic systems
AI summary Read the abstract
Researchers studied how natural macromolecules like humic acid, alginate, and proteins influence the clumping behavior of polystyrene nanoplastics in water. They found that these macromolecules generally stabilized nanoplastics in sodium chloride solutions but caused them to aggregate in calcium chloride solutions, with effects varying by pH. The findings suggest that the environmental fate and transport of nanoplastics in natural waters depends heavily on the surrounding organic molecules and water chemistry.
Research digests by email
When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.