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The weakened physiological functions of human serum albumin in presence of polystyrene nanoplastics

International Journal of Biological Macromolecules 2024 14 citations ? Citation count from OpenAlex, updated daily. May differ slightly from the publisher's own count.
Yaoyao Wang, Haimei Li, Jing Lan, Rui Guan, Yan Bao, Xianfa Du, Zongshan Zhao, Zongshan Zhao, Rongguang Shi, Henner Hollert, Xingchen Zhao

Summary

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.

Polymers
Study Type Environmental

Due to the widespread presence of nanoplastics (NPs) in daily essentials and drinking water, the potential adverse effects of NPs on human health have become a global concern. Human serum albumin (HSA), the most abundant and multi-functional protein in plasma, has been chosen to understand the biological effects of NPs after entering the blood. The esterase activity and the transport of bisphenol A in the presence of polystyrene nanoplastics (PSNPs) under physiological conditions (pH 4.0 and 7.4) have been investigated to evaluate the possible biological effects. The interactions between PSNPs and HSA have also been systematically studied by multispectral methods and dynamic light scattering techniques. The esterase activity of HSA presented a decreased trend with increasing PSNPs; conversely, higher permeabilities are accompanied by higher amounts of PSNPs. Compared with the unchanged hydrodynamic diameter and weaker interactions at pH 7.4, stronger binding between HSA and PSNPs at pH 4.0 led to a significant increase in the particle size of the PSNPs-HSA complex. The quenching mechanism belonged to the static quenching type. The electrostatic force is proposed to be the dominant factor for PSNPs binding to HSA. The work provides some information about the toxicity of NPs when exposed to humans.

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