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Surface interaction of vancomycin with polystyrene microplastics and its effect on human serum albumin
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Researchers studied how the antibiotic vancomycin interacts with polystyrene microplastics and what happens when that combination encounters human blood proteins. They found that vancomycin readily adsorbs onto microplastic surfaces, and that the resulting particle-drug complex can alter how the antibiotic binds to serum albumin in the blood. The study suggests that microplastics in the body could interfere with how medications are transported and function in the bloodstream.
Microplastics have a well-documented ability to adsorb various chemicals and contaminants found in the environment. By similar mechanisms, when medicines are stored in plastic packaging, the leaching of plastics into the contents poses the risk of possible toxicity and decreased drug efficacy. The work thus examines the presence of two categories of anthropogenic materials - microplastics (MPs) and medications - with their possible combined effects and fate in biological systems. A study on the kinetics and isotherm of the adsorption of vancomycin hydrochloride on the surface of polystyrene microspheres is performed, and the best-fitting models are obtained respectively as the pseudo-second-order model and the Temkin isotherm. Further, the interaction of each of, the drug, MPs and drug-adsorbed MPs with human serum albumin (HSA), the model protein chosen to validate the potential toxicity in humans, is determined by fluorescence spectroscopy. A thermodynamic analysis of this protein-ligand interaction shows that the process is spontaneous, endothermic and entropically favoured, and that hydrophobic forces operate between the interacting species. An unfolding of HSA is observed, disrupting its functions like the esterase activity. Competitive binding experiments with Warfarin and Ibuprofen as specific site markers on HSA reveal that all the studied ligands bind non-specifically to HSA.
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Researchers examined how the antibiotic clarithromycin binds to the surface of polystyrene nanoplastics and how this combination interacts with blood proteins. They found that the drug readily adsorbed onto the nanoplastic surface and that the drug-nanoplastic complex altered the structure and function of serum albumin more than either substance alone. The findings suggest that nanoplastics could amplify the biological effects of pharmaceutical pollutants by acting as carriers in the body.
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Researchers investigated how polystyrene nanoplastics interact with the antidiabetic drug metformin and how this combination affects binding to the human blood protein albumin. The study suggests that when metformin coats nanoplastic surfaces, it reduces the particles' affinity for albumin, potentially allowing nanoplastics to reach target organs and interfere with normal drug mechanisms in the body.
Molecular mechanisms of ciprofloxacin-loaded nanoplastics on human serum albumin: Protein denaturation and binding site recognition
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Scientists found that when tiny plastic particles (nanoplastics) team up with the antibiotic ciprofloxacin, the combo does more damage to a key blood protein called human serum albumin than either substance does alone, warping its shape and blocking its normal function. This matters because albumin helps carry nutrients, drugs, and hormones through your bloodstream, so this lab study suggests that pollution "cocktails" of plastics and antibiotics in the environment could pose a compounded health risk that we haven't been accounting for.
Nanoplastics alter the conformation and activity of human serum albumin
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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.
Unveiling the Modification of Esterase-like Activity of Serum Albumin by Nanoplastics and Their Cocontaminants
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Researchers investigated how polystyrene nanoplastics with different surface charges and sizes affect the enzymatic activity of human serum albumin, a key blood protein. The study found that amino-modified and smaller nanoplastics had the greatest impact on protein structure and inhibited its ability to metabolize compounds, while the presence of the drug metformin reduced nanoplastic binding to the protein. These findings suggest that nanoplastics could interfere with normal protein function in the bloodstream and that co-exposure with other chemicals may alter how nanoplastics are transported in the body.
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