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Citation
Tags
HERO ID
3860179
Reference Type
Journal Article
Title
Studies on the interaction of perfluorononanoic acid with human serum albumin by multi-spectroscopic, molecular docking and isothermal titration calorimetry techniques
Author(s)
Hu, TY; Huang, F; Zhou, SS; Liu, Y
Year
2016
Is Peer Reviewed?
Yes
Journal
Guangpuxue yu Guangpu Fenxi / Spectroscopy and Spectral Analysis
ISSN:
1000-0593
Location
China
Volume
36
Issue
12
Page Numbers
4141-4147
Language
English
PMID
30256599
DOI
10.3964/j.issn.1000-0593(2016)12-4141-07
Web of Science Id
WOS:000390613400058
URL
http://www.gpxygpfx.com/CN/abstract/abstract8871.shtml
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Abstract
Perfluorononanoic acid (PFNA) is the third most frequently detected in serum among all perfluoroalkyl acids (PFAAs) which is a kind of toxic emerging environmental contaminant. The influence of PFNA on the conformation and even function of human serum albumin (HSA) is still just at the beginning of research. The attempt of this paper was to completely elucidate the interaction mechanism of PFNA with HSA by means of multi-spectroscopic, molecular docking and isothermal titration calorimetry (ITC) techniques. The inner filter effect of all fluorescence data in the paper was eliminated to get accurate binding parameters. The results showed that the fluorescence of HSA was quenched by PFNA through a combined quenching procedure of dynamic and static quenching. Through site marker competitive experiments, subdomain IIA. of HSA had been assigned to possess the high-affinity binding site of PFNA. Furthermore, molecular docking reconfirmed that PFNA was bound in subdomain IIA mainly through polar force, hydrophobic interaction and halogen-bond, and the calculated free energy was -26.54 kJ.mol(-1) which indicated that the PFNA molecule exhibited large binding affinity towards HSA. The thermodynamic characterizations of two different classes of binding sites by ITC displayed that the first class with a higher affinity constant was dominated by an enthalpic contribution due to electrostatic interactions and halogen-bond, whereas the second class with a lower affinity constant was preponderated by hydrophobic interaction. The three-dimensional fluorescence revealed that the conformation of HSA was changed and the hydrophobicity of the Trp and Tyr residues microenvironment increased after formation of PFNA-HSA complex. The alterations of the protein secondary structure were quantitatively calculated from circular dichroism (CD) spectroscopy with reduction of a-helix content about 14.3%, beta-sheet 5.3%, beta-turn 3.5%, and augment in random content from 14.4% to 37.5%. Above results revealed that the binding of PFNA with HSA can alter the secondary structure of HSA, further probably affecting HSA physiological function. The results can provide insights with the binding mechanism of PFNA with HSA and salient biophysical and biochemical clues on elucidating the transport and distribution of PFNA in vivo.
Keywords
Perfluorononanoic acid; Human serum albumin; Multi-spectroscopic techniques; Molecular docking; Isothermal titration calorimetry
Tags
PFAS
•
5:3 acid
Literature Search
WOS
Screening Results
Excluded/Not on Topic
•
Additional PFAS (formerly XAgency)
Literature Search November 2019
Other Sources
TEDX
Screened Studies
Excluded
Exclude (TIAB)
•
Expanded PFAS SEM (formerly PFAS 430)
Litsearch: September 2019
Other Sources
PFAS TOX Database
Screened Studies
Excluded
Exclude (TIAB)
•
^Per- and Polyfluoroalkyl Substances (PFAS)
PFNA (375-95-1)
Literature Search
WOS
5:3 acid (914637-49-3)
Literature Search
WOS
•
PFAS 150
Literature Search August 2019
PubMed
Web of Science
Other sources
PFAS TOX Database
Not prioritized for screening
Perfluorononanoic acid
•
PFNA
Literature Search (August 2017)
Litsearch Addl Synonyms 2018
WOS
PFNA Literature Search pre-2019
Pubmed
WOS
Literature Search
WOS
Screening Results
In vitro/ex vivo/in silico
Protein binding
Title and Abstract Screening
Full Text Screening
Tagged as Supplemental
Mechanistic or MOA
ADME
In silico or modeling
June 2022 Pelch Database
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