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Investigation of the Interaction Mechanism of Perfluoroalkyl Carboxylic Acids with Human Serum Albumin by Spectroscopic Methods

School of Energy and Environmental Engineering, and Beijing Key Laboratory of Resource-oriented Treatment of Industrial Pollutants, University of Science and Technology Beijing, 30 Xueyuan Road, Haidian District, Beijing 100083, China
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Int. J. Environ. Res. Public Health 2020, 17(4), 1319; https://doi.org/10.3390/ijerph17041319
Received: 7 February 2020 / Revised: 13 February 2020 / Accepted: 15 February 2020 / Published: 18 February 2020
(This article belongs to the Section Environmental Science and Engineering)
Perfluoroalkyl carboxylic acids (PFCAs) are some of the most significant pollutants in human serum, and are reported to be potentially toxic to humans. In this study, the binding mechanism of PFCAs with different carbon lengths to human serum albumin (HSA) was studied at the molecular level by means of fluorescence spectroscopy under simulated physiological conditions and molecular modeling. Fluorescence data indicate that PFCAs with a longer carbon chain have a stronger fluorescence quenching ability. Perfluorobutanoic acid (PFBA) and perfluorohexanoic acid (PFHxA) had little effect on HSA. Fluorescence quenching of HSA by perfluorooctanoic acid (PFOA) and perfluorodecanoic acid (PFDA) was a static process that formed a PFCA–HSA complex. Electrostatic interactions were the main intermolecular forces between PFOA and HSA, while hydrogen bonding and van der Waals interactions played important roles in the combination of PFDA and HSA. In fact, the binding of PFDA to HSA was stronger than that of PFOA as supported by fluorescence quenching and molecular docking. In addition, infrared spectroscopy demonstrated that the binding of PFOA/PFDA resulted in a sharp decrease in the β-sheet and α-helix conformations of HSA. Our results indicated that the carbon chain length of PFCAs had a great impact on its binding affinity, and that PFCAs with longer carbon chains bound more strongly. View Full-Text
Keywords: perfluoroalkyl carboxylic acids (PFCAs); human serum albumin (HSA); fluorescence; toxicity; carbon chain length; molecular docking perfluoroalkyl carboxylic acids (PFCAs); human serum albumin (HSA); fluorescence; toxicity; carbon chain length; molecular docking
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MDPI and ACS Style

Chen, H.; Wang, Q.; Cai, Y.; Yuan, R.; Wang, F.; Zhou, B. Investigation of the Interaction Mechanism of Perfluoroalkyl Carboxylic Acids with Human Serum Albumin by Spectroscopic Methods. Int. J. Environ. Res. Public Health 2020, 17, 1319. https://doi.org/10.3390/ijerph17041319

AMA Style

Chen H, Wang Q, Cai Y, Yuan R, Wang F, Zhou B. Investigation of the Interaction Mechanism of Perfluoroalkyl Carboxylic Acids with Human Serum Albumin by Spectroscopic Methods. International Journal of Environmental Research and Public Health. 2020; 17(4):1319. https://doi.org/10.3390/ijerph17041319

Chicago/Turabian Style

Chen, Huilun, Qianyu Wang, Yanping Cai, Rongfang Yuan, Fei Wang, and Beihai Zhou. 2020. "Investigation of the Interaction Mechanism of Perfluoroalkyl Carboxylic Acids with Human Serum Albumin by Spectroscopic Methods" International Journal of Environmental Research and Public Health 17, no. 4: 1319. https://doi.org/10.3390/ijerph17041319

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