Structural evidence of perfluorooctane sulfonate transport by human serum albumin.
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TLDR
The crystal structure of the HSA-PFOS complex is reported and it is shown that PFOS binds to HSA at a molar ratio of 2:1, which provides a structural mechanism to understand the retention of surfactants in human serum.Abstract:
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.read more
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Risk to human health related to the presence of perfluorooctane sulfonic acid and perfluorooctanoic acid in food
Helle Katrine Knutsen,Jan Alexander,Lars Barregård,Margherita Bignami,Beat Johannes Brüschweiler,Sandra Ceccatelli,Bruce Cottrill,Michael Dinovi,Lutz Edler,Bettina Grasl-Kraupp,Christer Hogstrand,Laurentius Hoogenboom,Carlo Nebbia,Isabelle P. Oswald,Annette Petersen,Martin Rose,Alain-Claude Roudot,Christiane Vleminckx,Günter Vollmer,Heather M. Wallace,Laurent Bodin,Jean-Pierre Cravedi,Thorhallur I. Halldorsson,Line Småstuen Haug,Niklas Johansson,Henk Van Loveren,Petra Gergelova,Karen Mackay,Sara Levorato,Mathijs van Manen,Tanja Schwerdtle +30 more
TL;DR: For PFOS, the increase in serum total cholesterol in adults, and the decrease in antibody response at vaccination in children were identified as the critical effects and the CONTAM Panel established a tolerable weekly intake (TWI) of 13 ng/kg body weight (bw) per week for PFOS and 6 ng/ kg bw for PFOA.
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Interactive Association of Drugs Binding to Human Serum Albumin
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TL;DR: This review will succinctly outline the properties of binding site of drugs in IIA subdomain within the structure of HSA to give an overview on the binding characterization of interactive association of drugs to human serum albumin that may potentially lead to significant clinical applications.
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Bioaccumulation of Perfluorinated Alkyl Acids: Observations and Models
Carla A. Ng,Konrad Hungerbühler +1 more
TL;DR: It is concluded that the two prevailing hypotheses for the mechanisms that control the bioaccumulation of perfluorinated alkyl acids need not be mutually exclusive, but that protein interactions are needed to explain some important features of PFAA bio Accumulation.
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Perfluoroalkyl acid (PFAA) levels and profiles in breast milk, maternal and cord serum of French women and their newborns
Ronan Cariou,Bruno Veyrand,Ami Yamada,Alain Berrebi,Daniel Zalko,Sophie Durand,Charles Pollono,Philippe Marchand,Jean-Charles Leblanc,Jean-Philippe Antignac,Bruno Le Bizec +10 more
TL;DR: It is concluded that trans-placental passage and breastfeeding are both significant routes of human exposure to PFAAs and the estimated materno-foetal transfer would be thus substance-dependant, mainly driven by the physico-chemical properties of the different P FAAs.
Journal ArticleDOI
Isomer-Specific Binding Affinity of Perfluorooctanesulfonate (PFOS) and Perfluorooctanoate (PFOA) to Serum Proteins
TL;DR: Ultrafiltration devices provide a mechanistic explanation for the longer biological half-life of PFOS in humans, compared to PFOA, and for the higher transplacental transfer efficiencies and renal clearance of branched PFOS and P FOA isomers, comparedto the respective linear isomer.
References
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Xiao Min He,Daniel C. Carter +1 more
TL;DR: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.
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Journal ArticleDOI
Half-life of serum elimination of perfluorooctanesulfonate,perfluorohexanesulfonate, and perfluorooctanoate in retired fluorochemical production workers.
Geary W. Olsen,Jean M. Burris,David J. Ehresman,John W. Froehlich,Andrew M. Seacat,John L. Butenhoff,Larry R. Zobel +6 more
TL;DR: Humans appear to have a long half-life of serum elimination of PFOS, PFHS, and PFOA, which may be due, in part, to a saturable renal resorption process.
Journal ArticleDOI
Structural Basis of the Drug-Binding Specificity of Human Serum Albumin.
TL;DR: Crystallographic analysis of 17 different complexes of HSA with a wide variety of drugs and small-molecule toxins reveals the precise architecture of the two primary drug-binding sites on the protein, identifying residues that are key determinants of binding specificity and illuminating the capacity of both pockets for flexible accommodation.
Journal Article
The characterization of two specific drug binding sites on human serum albumin.
TL;DR: The binding of a number of fluorescent probe molecules to human serum albumin has been studied and changes in probe fluorescence were shown to be a result of competitive displacement by drugs.