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.