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Interaction of antidiabetic formulation with nanoplastics and its binary influence on plasma protein
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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.
Nanoplastics exposure to humans becomes inevitable due to its prevalence and permanence. Adsorption of emerging pollutant metformin hydrochloride (Met-HCl) -antidiabetic drug, on polystyrene nanoplastics (PSNPs) and influence on plasma protein binding was investigated. Fluorescence studies were carried out for human serum albumin (HSA) binding. Adsorption follows pseudo-second-order kinetics, intraparticle-diffusion, and Langmuir isotherm, undergoing both physisorption and chemisorption which was validated by FE-SEM, FTIR, and HRMS measurements. Complex, experiences static quenching mechanism by hydrogen bonding and VanderWaals force of attraction to HSA. FTIR confirms the secondary structural alteration of HSA. Since Met-HCl covers the NPs' surface, NPs' affinity for HSA is reduced and they might reach the target organs of Met-HCl, disrupt antidiabetic mechanisms and cause far-reaching implications. Results from molecular docking and simulation studies backed up these results as hydrophobic and hydrogen bonds dominate the binding process of the HSA-Met-HCl-PSNPs complex. This work will aid in understanding of the toxico-kinetics/dynamics of binary contaminants.
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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.
Adsorption of clarithromycin on polystyrene nanoplastics surface and its combined adverse effect on serum albumin
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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.
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.
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.
The weakened physiological functions of human serum albumin in presence of polystyrene nanoplastics
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Researchers found that polystyrene nanoplastics interfere with human serum albumin, the most abundant protein in blood that performs critical functions like transporting substances and acting as an enzyme. The nanoplastics reduced the protein's enzyme activity and altered its ability to transport chemicals like bisphenol A. This study provides evidence that once nanoplastics enter the human bloodstream, they could disrupt important blood protein functions with potential health consequences.
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