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Binding divergence of polystyrene nanoparticles with serum albumin caused by surface functionalization
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Researchers used multi-spectroscopy to show that surface functionalization of polystyrene nanoparticles determines how strongly they bind to human serum albumin — with carboxylated particles causing the greatest protein structural disruption and reduction in esterase activity, driven by differences in surface charge and hydrophobicity.
Using a combination of spectroscopy, we devised an integrated structural strategy to comprehensively profile the molecular details of the impact of differently functionalized (plain, aminated, and carboxylated) polystyrene nanoparticles (PSNPs) on human serum albumin (HSA). The binding isotherms obtained from fluorescence and UV-vis absorption measurements demonstrate that surface functionalization can distinguish the interaction of PSNPs with HSA. Three-dimensional fluorescence and circular dichroism analysis of the effect of interaction with PSNPs on the native conformation and secondary structures of the protein reveals a diminution in the skeleton structure of HSA induced by the PSNPs. In accordance with this, it is discovered that the esterase activity of protein-PSNPs aggregates is diminished compared to that of the native protein. The carboxylated PSNPs exhibited the strongest protein binding and perturbation effects compared to other particles. Plain PSNPs exhibited significant hydrophobic interaction properties, as evidenced by spectral blue shifts and a diminished Stokes shift in the three-dimensional fluorescence assay. Our results exclusively highlight that the hydrophobic and surface charge characteristics of PSNPs govern the extent of interaction with the protein, which is beneficial to understanding microplastic toxicology.
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When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.