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Probing the molecular mechanism of interaction between polystyrene nanoplastics and catalase by multispectroscopic techniques
Summary
Researchers investigated the molecular mechanism of interaction between polystyrene nanoplastics and the antioxidant enzyme catalase using multispectroscopic techniques, revealing how nanoplastic accumulation may disrupt enzymatic function and contribute to oxidative stress.
Nanoplastics are emerging pollutants that pose a potential threat to the environment and organisms and are widely distributed in environmental samples and food chains. The accumulation of polystyrene nanoplastics (PS-NPs) in an organism can cause oxidative stress. Currently, toxicity studies of PS-NPs mainly focus on the individual and cellular levels, whereas few studies have been conducted on the molecular mechanisms of the interaction between PS-NPs and catalase (CAT). Based on this, CAT was chosen as the target receptor for molecular toxicity research to reveal the interaction mechanism at the molecular level between PS-NPs and CAT by using various spectroscopic means and enzyme activity detection methods. The results indicated that PS-NPs destroyed the secondary structure of CAT, causing its protein skeleton to loosen and unfold, increasing the content of α-helices, decreasing the content of β-sheets, and exposing the position of the heme group. After exposure to PS-NPs, the internal fluorophore of CAT underwent fluorescence sensitization, resulting in a micelle-like structure, which enhanced the hydrophobicity of aromatic amino acids but did not change their polarity. In addition, the aggregation state of CAT was altered upon binding to PS-NPs, and the volume was further increased. Finally, these structural changes led to a gradual decrease in CAT activity. This study presents a comprehensive assessment of the toxicity of PS-NPs at the molecular level, which can provide more experimental support for the study of the biotoxicological efficacy of PS-NPs.