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The Formation of Protein Corona by Nanoplastics and Horseradish Peroxidase
Summary
Researchers investigated the formation of protein corona on amino-functionalized polystyrene nanoplastics by horseradish peroxidase, characterizing the adsorption interaction using multiple analytical approaches to understand how nanoplastics acquire protein coatings in biological environments. They found that nanoplastics readily adsorb the enzyme to form a stable protein corona, which may alter both nanoplastic behavior in biological systems and enzyme activity.
In theory, nanoplastics (NPs) can adsorb biological macromolecules, such as proteins, in the surrounding environment to form protein corona (PC). In this study, we focus on amino polystyrene (PS) NPs and horseradish peroxidase (HRP) to explore the dynamic process of the formation of PS-HRP PC and their influence on PS and HRP. This work used atomic force microscopy, laser particle size and Zeta potential analyzer, and UV-vis spectrophotometer. According to the adsorption behavior of HRP to NPs, the surface morphology characteristics of NPs can be observed to change at 60 min. Meanwhile, the increase in size and hydrodynamic diameter, the decrease in Zeta potential, surface roughness and HRP activity, and the change in HRP structure attest to the PC formation. The thickness of the PC was approximately 30 nm and there are differences in the dynamic and static variations in the size of the PC. The PC formation process progresses gradually from 0 min to 240 min. Overall, the formation of PS-HRP PC is identified, and the changes in its properties are confirmed from the perspective of nanoplastics and peroxidase, which help study the effects of nanoplastics on the environment and creatures.
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