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New Molecular Mechanism of Nanoplastics Affecting Cadmium Protein Toxicity: Conformational Response and Differential Binding of Human Serum Albumin
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New molecular mechanism of nanoplastics affecting cadmium protein toxicity: Conformational response and differential binding of human serum albumin
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Researchers showed that cadmium alone disrupts the structure and transport function of human serum albumin (the blood's main protein carrier), and that co-exposure with nanoplastics — which form a protein corona by binding albumin to their surface — further exacerbates these structural disruptions and enzyme activity losses, raising concerns about combined nanoplastic-heavy metal toxicity.
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Researchers used spectroscopy, enzyme assays, and computational modeling to show that nanoplastics form a protein corona around cadmium ions that enhances cadmium's structural disruption of trypsin, causing enzyme overactivation (227% of baseline) — a mechanism by which nanoplastics can amplify the toxicity of co-occurring heavy metals on digestive proteins.
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Laboratory experiments found that biodegradable polylactic acid (PLA) microplastics adsorb significant amounts of cadmium, and simulated gastrointestinal digestion dramatically increased cadmium bioaccessibility — 19% released in the gastric phase and 62% in the intestinal phase — far exceeding conventional PP and PA microplastics. This indicates that biodegradable plastics marketed as environmentally safer alternatives may pose heightened risks as heavy metal vectors in the human gut, challenging assumptions about their safety.
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Researchers exposed mice to cadmium and polystyrene nanoplastics individually and together, finding that co-exposure synergistically worsened kidney damage by activating PANoptosis — a coordinated cell death cascade integrating pyroptosis, apoptosis, and necroptosis — with the scaffold protein ASC markedly upregulated as a central driver.
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