Structural Evidence of Perfluorooctane Sulfonate Transport by Human Serum Albumin

Perfluorooctane sulfonate (PFOS) is a man-made fluorosurfactant and globally persistent organic pollutant. PFOS is mainly distributed in blood with a long half-life for elimination. PFOS was found mainly bound to human serum albumin (HSA) in plasma, the most abundant protein in human blood plasma, w...

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Published inChemical research in toxicology Vol. 25; no. 5; pp. 990 - 992
Main Authors Luo, Zhipu, Shi, Xiaoli, Hu, Qin, Zhao, Bin, Huang, Mingdong
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 21.05.2012
Subjects
Alkanesulfonic Acids - chemistry
Alkanesulfonic Acids - metabolism
Binding Sites
Crystallography, X-Ray
Fluorocarbons - chemistry
Fluorocarbons - metabolism
Humans
Models, Molecular
Protein Binding
Serum Albumin - chemistry
Serum Albumin - metabolism
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Summary:Perfluorooctane sulfonate (PFOS) is a man-made fluorosurfactant and globally persistent organic pollutant. PFOS is mainly distributed in blood with a long half-life for elimination. PFOS was found mainly bound to human serum albumin (HSA) in plasma, the most abundant protein in human blood plasma, which transports a variety of endogenous and exogenous ligands. However, the structural basis of such binding remains unclear. Here, we report the crystal structure of the HSA–PFOS complex and show that PFOS binds to HSA at a molar ratio of 2:1. In addition, PFOS binding renders the HSA structure more compact. Our results provide a structural mechanism to understand the retention of surfactants in human serum.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0893-228X
1520-5010
DOI:10.1021/tx300112p