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Probing the toxic interactions between polyvinyl chloride microplastics and Human Serum Albumin by multispectroscopic techniques
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Scientists used multiple spectroscopic techniques to characterize how PVC microplastics interact with human serum albumin (the most abundant protein in blood), finding that PVC binds to albumin, alters its structure, and may affect the protein's ability to carry drugs and nutrients.
In this study, the interaction of emerging pollutant polyvinyl chloride microplastics (PVC MPs) and human serum albumin (HSA) was investigated by fluorescence spectroscopy, UV-visible (UV-vis) absorption spectroscopy, circular dichroism (CD), and Fourier transform infrared (FT-IR) spectroscopy under simulated physiological conditions. Fluorescence results showed that PVC MPs (about 5000 nm in size) can effectively quench the intrinsic fluorescence of HSA through static quenching owing to the formation of HSA-PVC complex. The binding constants (K) between PVC and HSA at different temperatures were calculated as 4.97 × 10 M, 3.46 × 10 M and 2.51 × 10 M, respectively. The number of binding sites was 1.26. The enthalpy change (ΔH), entropy change (ΔS) and free energy change (ΔG) were calculated to be -59.27 kJ·mol, 70.76 J·mol K and - 80.35 kJ·mol, respectively, indicating that the interaction of PVC with HSA was mainly driven by electrostatic forces. Moreover, results of UV-vis, FT-IR and CD further demonstrated that the microenvironment and secondary structure of HSA were changed a lot induced by PVC, leading to a decrease in α-helix. This work not only provides an insight into the intermolecular interaction between PVC and HSA, but also elucidates the potential biological toxicity of MPs at a molecular level.
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Researchers investigated the binding interaction between polyvinyl chloride microplastics and bovine serum albumin using multiple spectroscopic techniques, finding that PVC MPs bind to BSA through hydrophobic interactions and alter the protein's secondary structure, suggesting potential implications for protein function in biological systems.
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Researchers investigated how polystyrene nanoplastics interact with human serum albumin, a key blood protein, and found that nanoplastics bind to the protein through hydrophobic forces, altering its structure and reducing its enzymatic activity. The study suggests that nanoplastic exposure could interfere with normal protein function in the bloodstream, highlighting the need for regulation of nanoplastics in consumer products.
Microplastics-Induced Binding and Structural Changes in the Milk Proteins: α -Lactalbumin and β -Lactoglobulin
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Researchers used multispectroscopic methods to show that PVC, PE, and PS microplastics bind strongly to the milk whey proteins α-lactalbumin and β-lactoglobulin under physiological conditions, altering their secondary structures and triggering amyloid fibril formation, with implications for how microplastics transferred to breast milk could affect protein function.
Interactions of nanoplastics with human albumin and hemoglobin: Structural and spectroscopic insights
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Scientists found that tiny plastic particles (nanoplastics) can physically attach to two key proteins in human blood, albumin and hemoglobin (the protein that carries oxygen), and actually change their shape. This matters because a protein's shape determines how well it works in the body, so these changes could potentially affect how blood proteins function, though more research is needed to confirm real-world health effects. It's an early but important clue in understanding how the plastic pollution we're increasingly exposed to might interact with our bodies at the molecular level.
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