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Spectroscopic investigations on the interaction between nano plastic and catalase on molecular level
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Researchers investigated how polystyrene nanoplastics interact with the enzyme catalase at different pH levels, finding that nanoplastics alter the protein's secondary structure and reduce its enzymatic activity through static quenching and hydrophobic binding mechanisms.
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.
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