Binding Affinity and Mechanism of Six PFAS with Human Serum Albumin: Insights from Multi-Spectroscopy, DFT and Molecular Dynamics Approaches.

ABSTRACT: Per- and Polyfluoroalkyl Substances (PFAS) bioaccumulate in the human body, presenting potential health risks and cellular toxicity. Their transport mechanisms and interactions with tissues and the circulatory system require further investigation. This study investigates the interaction mechanisms of six PFAS with Human Serum Albumin (HSA) using multi-spectroscopy, DFT and a molecular dynamics approach. Multi-spectral analysis shows that perfluorononanoic acid (PFNA) has the best binding capabilities with HSA. The order of binding constants (298 K) is as follows: "Perfluorononanoic Acid (PFNA, 7.81 × 10⁶ L·mol^-1) > Perfluoro-2,5-dimethyl-3,6-dioxanonanoic Acid (HFPO-TA, 3.70 × 10⁶ L·mol^-1) > Perfluorooctanoic Acid (PFOA, 2.27 × 10⁵ L·m

SUBMITTER: Peng M 

PROVIDER: S-EPMC10819430 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature