Journal
CHEMOSPHERE
Volume 198, Issue -, Pages 442-449Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.chemosphere.2018.01.152
Keywords
Perfluorooctanoic acid (PFOA); Perfluorooctanesulfonic acid (PFOS); Protein complexes; Serum albumins; Native mass spectrometry
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Funding
- National Natural Science Foundation of China [21675176, 21275167]
- Natural Science Foundation of Hubei Province [2014CFA025]
- Fundamental Research Funds for the Central Universities, South-Central University of Nationalities [CTZ13008]
- Preferred Research Foundation for the Returned Overseas Scholars from Ministry of Human Resources and Social Security of the People's Republic of China
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The binding information of perfluorooctanoic acid (PFOA) and perfluorooctanesulfonic acid (PFOS) with bovine and human serum albumins was investigated and characterized in details by using a combination method of electrospray ionization mass spectrometry (ESI-MS), fluorescence, circular dichroism (CD) and molecular docking (MD). The ESI-MS analysis revealed that maximally eight PFOA or PFOS molecules could bind to serum albumins at high mole ratios of PFOA/PFOS. Association constants were measured by ESI-MS and suggested that PFOS had a better binding affinity than PFOA. PFOA and PFOS were likely to bind with serum albumins in more than one pocket. The CD data demonstrated that binding of PFOA and PFOS could change the conformation of serum albumins with decreasing alpha-helix content, which may affect the protein physiological function. The phenomenon of protein fluorescence quenching by the binding of PFOA and PFOS indicated that the hydrophobic pocket proximate to Trp 214 in human serum albumin might be one of the dominated binding sites. This assumption was further confirmed by MD simulation. Consistent to ESI-MS observation, MD results also displayed a stronger binding affinity of PFOS than PFOA according to the calculated binding free energy, which is probably ascribed to one more hydrogen bond formed in the PFOS-bound protein complexes. (C) 2018 Elsevier Ltd. All rights reserved.
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