Jump to main content
US EPA
United States Environmental Protection Agency
Search
Search
Main menu
Environmental Topics
Laws & Regulations
About EPA
Health & Environmental Research Online (HERO)
Contact Us
Print
Feedback
Export to File
Search:
This record has one attached file:
Add More Files
Attach File(s):
Display Name for File*:
Save
Citation
Tags
HERO ID
4238332
Reference Type
Journal Article
Title
Interactions of perfluorooctanoic acid and perfluorooctanesulfonic acid with serum albumins by native mass spectrometry, fluorescence and molecular docking
Author(s)
Chi, Q; Li, Z; Huang, J; Ma, J; Wang, X
Year
2018
Is Peer Reviewed?
Yes
Journal
Chemosphere
ISSN:
0045-6535
EISSN:
1879-1298
Volume
198
Page Numbers
442-449
Language
English
PMID
29425944
DOI
10.1016/j.chemosphere.2018.01.152
Web of Science Id
WOS:000427338800051
Abstract
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 α-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.
Keywords
perfluorooctanoic acid (PFOA); perfluorooctanesulfonic acid (PFOS); protein complexes; serum albumins; native mass spectrometry
Tags
PFAS
•
Additional PFAS (formerly XAgency)
•
Expanded PFAS SEM (formerly PFAS 430)
Litsearch: September 2019
PubMed
Not prioritized for screening
Perfluorooctane
Potassium perfluorooctanoate
Sodium perfluorooctanoate
•
PFAS 150
Literature Search Update December 2020
PubMed
WOS
Literature Search August 2019
PubMed
Web of Science
Not prioritized for screening
Ammonium perfluorooctanoate
Perfluorinated compounds
Perfluorooctane
Perfluorooctanesulfonic acid
Perfluorooctanoic acid
•
PFHxS
•
PFNA
Litsearch Update 2017-2018
Pubmed
Literature Search
Pubmed
•
PFOA (335-67-1) and PFOS (1763-23-1)
Literature Search Update (2013-2019)
PubMed
WOS
Home
Learn about HERO
Using HERO
Search HERO
Projects in HERO
Risk Assessment
Transparency & Integrity