Serum albumin mitigated perfluorooctane sulfonate-induced cytotoxicity by affecting the cellular responses

Ya-Di Yang; Jia-Xin Li; Naihao Lu; Rong Tian

doi:10.1016/j.bpc.2023.107110

Serum albumin mitigated perfluorooctane sulfonate-induced cytotoxicity by affecting the cellular responses

Biophys Chem. 2023 Nov:302:107110. doi: 10.1016/j.bpc.2023.107110. Epub 2023 Sep 18.

Authors

Ya-Di Yang¹, Jia-Xin Li¹, Naihao Lu¹, Rong Tian²

Affiliations

¹ Jiangxi Key Laboratory of Green Chemistry, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, China.
² Jiangxi Key Laboratory of Green Chemistry, College of Chemistry and Chemical Engineering, Jiangxi Normal University, Nanchang 330022, China. Electronic address: tianrong@jxnu.edu.cn.

PMID: 37741269
DOI: 10.1016/j.bpc.2023.107110

Abstract

During the wide applications of perfluorinated materials such as perfluorooctane sulfonate (PFOS) in commercial and industrial products, the potential toxicity of these engineered compounds has attracted more and more attention. As a typical environmental pollutant, PFOS could preferentially bind to albumin protein in vivo. However, the role of protein-PFOS interactions in the cytotoxicity of PFOS was not stressed enough. Herein, we investigated the interactions of PFOS with human serum albumin (HSA, the most abundant protein in human plasma) using both experimental and theoretical approaches. It was demonstrated that PFOS could mainly bind to the Sudlow site I of HSA to generate HSA-PFOS complex through hydrogen bonds and van der Waals forces. Toxicity assays with endothelial cells illustrated that the binding of HSA could significantly attenuate the intracellular uptake and subcellular distribution of PFOS, thereby inhibiting the formation of reactive oxygen species and toxicity for those HSA-bound PFOS. Similarly, the presence of fetal bovine serum in the cell culture media greatly reduced PFOS-caused cytotoxicity. Conclusively, our study reveals that the binding of albumin protein to PFOS could mitigate its toxicity by the modulation of cellular responses. The formation of protein-complexed contaminants would significantly reduce the bioavailability of these chemicals and subsequently mitigate their environmental toxicology to the human health.

Keywords: Cytotoxicity; Interaction; Perfluorooctane sulfonate; Serum albumin.