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Study on the binding of polystyrene microplastics with superoxide dismutase at the molecular level by multi-spectroscopy methods
Summary
Researchers used multiple spectroscopy methods to study how polystyrene microplastics interact with the antioxidant enzyme superoxide dismutase (SOD) at the molecular level. The study found that microplastics altered SOD's protein structure, forming larger complexes and increasing the enzyme's activity in a concentration-dependent manner, providing insights into how microplastics may affect biological antioxidant systems.
Microplastics are harmful pollutants that widely exist worldwide and pose a severe threat to all types of organisms. The effects of polystyrene microplastics (PS-MPs) on organisms have been extensively studied, but the interaction mechanism between PS-MPs and superoxide dismutase (SOD) at the molecular level has not been reported yet. Therefore, based on multiple spectroscopic methods and enzyme activity measurements, the molecular mechanism of the interaction between PS-MPs and SOD was investigated. The multispectral results showed that the protein skeleton and secondary structure of SOD were altered by PS-MPs, resulting in decreased α-helix and β-sheet content. After PS-MPs exposure, fluorescence sensitization occurred, and micelles were formed, along with the enhanced hydrophobicity of aromatic amino acids in SOD. Moreover, the resonance light scattering (RLS) spectra result suggested that the PS-MPs and SOD combined to form a larger complex. Eventually, the activity of SOD was increased due to these structural changes, and the concentration of PS-MPs is positively correlated with SOD activity. This study can provide experimental support for studying the toxicological effects of PS-MPs.