Interaction of polystyrene nanoplastics and hemoglobin is determined by both particle curvature and available surface area.

Understanding nanoplastic (NP, or nanoparticle in general) toxicity requires establishing the causal relationships between the physical properties of the nanoparticles and their biological impact. We use spectroscopic, zeta-potential, and dynamic light scattering (DLS) techniques to investigate the formation, structure, and catalytic properties of hemoglobin corona complexes with polystyrene NPs (0-10 mg/mL) of various diameters (20, 50, 100, 500, and 5000 nm). Resonance light scattering, zeta-potential analysis, and DLS demonstrated that hemoglobin corona complexes formed different forms of aggregates with NPs in terms of diameter. Medium-sized (100 nm) NPs induced the most significant conformational alterations in the protein corona compared to smaller and larger ones, which was revealed by spectroscopic assays. However, the catalase-like activity of hemoglobin was promoted in the presence of 100 nm NPs by as high as 35.2 %. NP curvature and surface area are antagonistic factors that govern the conformation of proteins together. This also suggests that 100 nm NPs are more likely to disrupt protein-dependent physiological processes at a given mass concentration than small or large NPs.

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, 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.

Spectroscopic investigations on the interaction between nano plastic and catalase on molecular level.

As an emerging pollutant that is easily bonded with some functional proteins and the effects of their physiological expressions, nano plastics (NPs) have been widely detected in various environmental mediums, even in human blood. Compared to microplastics, less information on the interactions between NPs and proteins has been reported. Here, the interaction mechanism between common polystyrene nano plastics (PSNPs) and catalase (CAT) under two typical physiological conditions, pH 7.4 and 4.0, was investigated by UV-visible spectroscopy, circular dichroism (CD), and dynamic light scattering (DLS). Compared with the enhanced catalytic effects when increasing PSNPs at pH 7.4, a trend of initial inhibition and enhanced activity was observed at pH 4.0. Spectroscopic analysis and calculation results indicated that their binding was static, with only one binding site and stronger interactions under acidic conditions. UV-visible and CD spectra analysis demonstrated that the difference in enzymatic activity could be mainly attributed to the conformational alternation of CAT in the presence of PSNPs, which is obviously affected by solution chemistry. The change was also revealed by the hydrodynamic diameter and zeta potentials of the complexes supplied by DLS analysis. This study will help understand the health risks of nano plastic pollution and provide a theoretical basis for studying their toxicological effects.