We can't find the internet
Attempting to reconnect
Something went wrong!
Hang in there while we get back on track
Adsorption of clarithromycin on polystyrene nanoplastics surface and its combined adverse effect on serum albumin
AI summary Read the abstract
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.
Emerging contaminants, such as antibiotics and nanoplastics, have garnered significant attention due to their potential adverse effects on diverse ecosystems. Antibiotic adsorption on the surface of nanoplastics potentially facilitates their long-range transport, leading to the synergistic effects of the complex. This research aims to examine the adsorption behavior of clarithromycin binding with polystyrene nanoplastics surface as well as their interaction between drug adsorbed polystyrene nanoplastics with serum albumin. Different spectroscopic methods were used to find out the interaction between clarithromycin and nanoplastics, under stimulated physiological conditions UV-vis spectroscopy showed a maximum of 22.8% percentage of the drug adsorbed with the polystyrene nanoplastics surface after 6 h of incubation. The fluorescence spectroscopic results demonstrated that the fluorescence intensity of serum albumin was quenched by the clarithromycin-polystyrene nanoplastics (CLA-PSNP) complex through static quenching. We calculated the number of binding stoichiometry, binding constants, and thermodynamic parameters. This study revealed that the CLA-PSNP binds to serum albumin spontaneously and its hydrophobic interactions played a significant role. The conformational changes in the structure of serum albumin were revealed from the findings of synchronous fluorescence spectra, CD spectra, and 3D fluorescence spectra, leading to the disturbance in functional activity. This study focuses valuable insights into the intermolecular interactions between clarithromycin-adsorbed polystyrene nanoplastics and serum albumin and its potential molecular-level biological toxicity.
More Papers Like This
Surface interaction of vancomycin with polystyrene microplastics and its effect on human serum albumin
AI summary Read the abstract
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.
Investigating the impact of nanoplastics in altering the efficacy of clarithromycin antibiotics through In vitro studies
AI summary Read the abstract
Researchers investigated how polystyrene nanoplastics interact with the antibiotic clarithromycin and affect both insulin structure and bacterial resistance. They found that nanoplastics can adsorb the antibiotic, leading to structural changes in insulin that could potentially contribute to insulin resistance, while also reducing the antibiotic's ability to inhibit pathogenic bacteria. The findings highlight the complex ways nanoplastics may interfere with pharmaceutical efficacy.
Interaction of antidiabetic formulation with nanoplastics and its binary influence on plasma protein
AI summary Read the abstract
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 alter the conformation and activity of human serum albumin
AI summary Read the abstract
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
AI summary Read the abstract
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.
Research digests by email
When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.