Adsorption of clarithromycin on polystyrene nanoplastics surface and its combined adverse effect on serum albumin

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. [Display omitted] •Clarithromycin adsorbs on polystyrene nanoplastics (PSNP) in the environment.•Adsorption behavior of clarithromycin is characterized and confirmed by UV, DLS, FE-SEM, FTIR, and HRMS analysis.•Binary pollutant enters the human as well as bovine bloodstream.•CLA-PSNP (binary complex) binds with serum albumin.•CLA-PSNP causes conformational changes in the secondary structure of serum albumin.