Article
?
AI-assigned paper type based on the abstract. Classification may not be perfect — flag errors using the feedback button.
Tier 2
?
Original research — experimental, observational, or case-control study. Direct primary evidence.
Sign in to save
Surface interaction of vancomycin with polystyrene microplastics and its effect on human serum albumin
International Journal of Biological Macromolecules2023
15 citations
?
Citation count from OpenAlex, updated daily. May differ slightly from the publisher's own count.
Score: 55
?
0–100 AI score estimating relevance to the microplastics field. Papers below 30 are filtered from public browse.
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.