In Vitro and In Silico Analysis of the Bindings between Legacy and Novel Per- and Polyfluoroalkyl Substances and Human Serum Albumin

Per- and polyfluoroalkyl substances (PFASs) are emerging contaminants of concern that can enter the human body through a variety of pathways and thereby cause harmful effects. Exposure of pregnant women to PFASs could even affect both the mother and the child. Human serum albumin (HSA) is considered...

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Main Authors: Yuqing Wu, Jia Bao, Yang Liu, Xin Wang, Xinyi Lu, Ke Wang
Format: Article
Language:English
Published: MDPI AG 2024-01-01
Series:Toxics
Subjects:
Online Access:https://www.mdpi.com/2305-6304/12/1/46
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author Yuqing Wu
Jia Bao
Yang Liu
Xin Wang
Xinyi Lu
Ke Wang
author_facet Yuqing Wu
Jia Bao
Yang Liu
Xin Wang
Xinyi Lu
Ke Wang
author_sort Yuqing Wu
collection DOAJ
description Per- and polyfluoroalkyl substances (PFASs) are emerging contaminants of concern that can enter the human body through a variety of pathways and thereby cause harmful effects. Exposure of pregnant women to PFASs could even affect both the mother and the child. Human serum albumin (HSA) is considered to be the primary transport protein for a variety of substances in body fluids. It can be bound to different contaminants and might result in possible effects on human health. Yet, few studies are available on the binding affinity of legacy PFASs and their novel alternatives to HSA. In this study, the binding mechanisms of HSA to both legacy PFASs and their novel alternatives were investigated using fluorescence spectroscopy, together with further molecular docking. The results show that all the target PFASs were statically quenched against HSA with binding ratios of 1:1. The binding constants of long-chain PFASs and novel alternatives of perfluoroalkanesulfonic acids (PFSAs) were greater than 10<sup>2</sup>, whereas those of short-chain PFASs alternatives and novel alternatives of perfluorocarboxylic acids (PFCAs) were less than 10<sup>2</sup>. In general, the binding affinities of PFCAs on HSA were less than that of PFSAs, while the binding affinities of short-chain PFASs alternatives on HSA were smaller than those of long-chain PFASs and their novel alternatives. Therefore, bindings to HSA could be considered as an important influencing factor for the bioaccumulation of legacy and novel PFASs in the human body.
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spelling doaj.art-963ba6fcb6fb455dad63a4eafb51f44f2024-01-26T18:41:10ZengMDPI AGToxics2305-63042024-01-011214610.3390/toxics12010046In Vitro and In Silico Analysis of the Bindings between Legacy and Novel Per- and Polyfluoroalkyl Substances and Human Serum AlbuminYuqing Wu0Jia Bao1Yang Liu2Xin Wang3Xinyi Lu4Ke Wang5School of Environmental and Chemical Engineering, Shenyang University of Technology, Shenyang 110870, ChinaSchool of Environmental and Chemical Engineering, Shenyang University of Technology, Shenyang 110870, ChinaSchool of Environmental and Chemical Engineering, Shenyang University of Technology, Shenyang 110870, ChinaSchool of Environmental and Chemical Engineering, Shenyang University of Technology, Shenyang 110870, ChinaSchool of Environmental and Chemical Engineering, Shenyang University of Technology, Shenyang 110870, ChinaDepartment of Clinical Nutrition, Second Affiliated Hospital of Dalian Medical University, Dalian 116023, ChinaPer- and polyfluoroalkyl substances (PFASs) are emerging contaminants of concern that can enter the human body through a variety of pathways and thereby cause harmful effects. Exposure of pregnant women to PFASs could even affect both the mother and the child. Human serum albumin (HSA) is considered to be the primary transport protein for a variety of substances in body fluids. It can be bound to different contaminants and might result in possible effects on human health. Yet, few studies are available on the binding affinity of legacy PFASs and their novel alternatives to HSA. In this study, the binding mechanisms of HSA to both legacy PFASs and their novel alternatives were investigated using fluorescence spectroscopy, together with further molecular docking. The results show that all the target PFASs were statically quenched against HSA with binding ratios of 1:1. The binding constants of long-chain PFASs and novel alternatives of perfluoroalkanesulfonic acids (PFSAs) were greater than 10<sup>2</sup>, whereas those of short-chain PFASs alternatives and novel alternatives of perfluorocarboxylic acids (PFCAs) were less than 10<sup>2</sup>. In general, the binding affinities of PFCAs on HSA were less than that of PFSAs, while the binding affinities of short-chain PFASs alternatives on HSA were smaller than those of long-chain PFASs and their novel alternatives. Therefore, bindings to HSA could be considered as an important influencing factor for the bioaccumulation of legacy and novel PFASs in the human body.https://www.mdpi.com/2305-6304/12/1/46PFASsalternativeshuman serum albuminbindingfluorescence spectroscopymolecular docking
spellingShingle Yuqing Wu
Jia Bao
Yang Liu
Xin Wang
Xinyi Lu
Ke Wang
In Vitro and In Silico Analysis of the Bindings between Legacy and Novel Per- and Polyfluoroalkyl Substances and Human Serum Albumin
Toxics
PFASs
alternatives
human serum albumin
binding
fluorescence spectroscopy
molecular docking
title In Vitro and In Silico Analysis of the Bindings between Legacy and Novel Per- and Polyfluoroalkyl Substances and Human Serum Albumin
title_full In Vitro and In Silico Analysis of the Bindings between Legacy and Novel Per- and Polyfluoroalkyl Substances and Human Serum Albumin
title_fullStr In Vitro and In Silico Analysis of the Bindings between Legacy and Novel Per- and Polyfluoroalkyl Substances and Human Serum Albumin
title_full_unstemmed In Vitro and In Silico Analysis of the Bindings between Legacy and Novel Per- and Polyfluoroalkyl Substances and Human Serum Albumin
title_short In Vitro and In Silico Analysis of the Bindings between Legacy and Novel Per- and Polyfluoroalkyl Substances and Human Serum Albumin
title_sort in vitro and in silico analysis of the bindings between legacy and novel per and polyfluoroalkyl substances and human serum albumin
topic PFASs
alternatives
human serum albumin
binding
fluorescence spectroscopy
molecular docking
url https://www.mdpi.com/2305-6304/12/1/46
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