Unveiling the Modification of Esterase-like Activity of Serum Albumin by Nanoplastics and Their Cocontaminants.

Abstract

Nanoplastics and other cocontaminants have raised concerns due to their widespread presence in the environment and their potential to enter the food chain. The harmful effects of these particles depend on various factors, such as nanoparticle size, shape, surface charge, and the nature of the cocontaminants involved. On entering the human body, human serum albumin (HSA) molecules bind and transport these particles in the blood system. The esterase-like activity of HSA, which plays a role in metabolizing drug/toxic compounds, was taken as a representative to portray the effects of these particles on HSA. Polystyrene nanoplastics (PSNPs) with different surface functionalization (plain (PS), amine (PS-NH2), and carboxy (PS-COOH)), different sizes (100 and 500 nm), and PS with cocontaminant metformin hydrochloride (Met-HCl), a widely used antidiabetic drug, were investigated in this study. Fluorescence emission spectra of HSA revealed that PS-NH2 exhibits a greater effect on protein conformation, smaller NPs have a greater influence on protein structure than larger NPs, and Met-HCl lowers PSNPs' affinity for HSA by coating the surface of the NPs, which may result in direct NP distribution to the drug's target organs and toxicity. Circular dichroism spectra also supported these results in terms of secondary structural changes. Esterase activity of HSA was inhibited by all the particles (except Met-HCl) by competitive inhibition as concluded from constant Vmax and increasing Km. Greater reduction in enzyme activity was observed for PS-NH2 among functionalizations and for 100 nm PS among sizes. Furthermore, Met-HCl lowers the inhibitory impact of PSNPs on HSA since the drug binds weakly to HSA, and so they can serve as a vector delivering PSNPs to their target organs, resulting in serious implications.