Interaction studies of polybrominated diphenyl ethers (PBDEs) with human serum albumin (HSA): Molecular docking investigations

Songwen Tan; Zhenxing Chi; Ye Shan; Zhengzhong Wen; Weiguo Li

doi:10.1016/j.etap.2017.06.005

Interaction studies of polybrominated diphenyl ethers (PBDEs) with human serum albumin (HSA): Molecular docking investigations

Songwen Tan
, Zhenxing Chi^*
, Ye Shan
, Zhengzhong Wen
, Weiguo Li

^*Corresponding author for this work

School of Marine Science and Technology

Harbin Institute of Technology Weihai
Jinan University

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

This work has evaluated the interactions of HSA and typical PBDEs (BDE47, BDE99, BDE100, BDE153 and BDE209) at molecular level by modelling. Apart from the BDE209, PBDEs with higher molecular weight show higher binding energy with the residues of HSA. The BDE209 without H atoms has the lowest binding energy (-ΔG_binding: 4.30 cal mol⁻¹) than other PBDEs (-ΔG_binding: 7.93–8.42 cal mol⁻¹). The BDE99 shows a higher binding energy than its isomer (BDE100). On the other hand, the lgK_ow-depth plotting figure shows that a higher K_ow value (hydrophobicity) of PBDEs is accompanied by a deeper binding site within the central channel of HSA. This work may provide a theoretical method to assess the transport and distribution of PBDEs in human body.

Original language	English
Pages (from-to)	34-39
Number of pages	6
Journal	Environmental Toxicology and Pharmacology
Volume	54
DOIs	https://doi.org/10.1016/j.etap.2017.06.005
State	Published - Sep 2017

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Binding depth
Human serum albumin
Molecule docking
Polybrominated diphenyl ethers

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10.1016/j.etap.2017.06.005

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title = "Interaction studies of polybrominated diphenyl ethers (PBDEs) with human serum albumin (HSA): Molecular docking investigations",

abstract = "This work has evaluated the interactions of HSA and typical PBDEs (BDE47, BDE99, BDE100, BDE153 and BDE209) at molecular level by modelling. Apart from the BDE209, PBDEs with higher molecular weight show higher binding energy with the residues of HSA. The BDE209 without H atoms has the lowest binding energy (-ΔGbinding: 4.30 cal mol−1) than other PBDEs (-ΔGbinding: 7.93–8.42 cal mol−1). The BDE99 shows a higher binding energy than its isomer (BDE100). On the other hand, the lgKow-depth plotting figure shows that a higher Kow value (hydrophobicity) of PBDEs is accompanied by a deeper binding site within the central channel of HSA. This work may provide a theoretical method to assess the transport and distribution of PBDEs in human body.",

keywords = "Binding depth, Human serum albumin, Molecule docking, Polybrominated diphenyl ethers",

author = "Songwen Tan and Zhenxing Chi and Ye Shan and Zhengzhong Wen and Weiguo Li",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier B.V.",

year = "2017",

month = sep,

doi = "10.1016/j.etap.2017.06.005",

language = "英语",

volume = "54",

pages = "34--39",

journal = "Environmental Toxicology and Pharmacology",

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TY - JOUR

T1 - Interaction studies of polybrominated diphenyl ethers (PBDEs) with human serum albumin (HSA)

T2 - Molecular docking investigations

AU - Tan, Songwen

AU - Chi, Zhenxing

AU - Shan, Ye

AU - Wen, Zhengzhong

AU - Li, Weiguo

PY - 2017/9

Y1 - 2017/9

N2 - This work has evaluated the interactions of HSA and typical PBDEs (BDE47, BDE99, BDE100, BDE153 and BDE209) at molecular level by modelling. Apart from the BDE209, PBDEs with higher molecular weight show higher binding energy with the residues of HSA. The BDE209 without H atoms has the lowest binding energy (-ΔGbinding: 4.30 cal mol−1) than other PBDEs (-ΔGbinding: 7.93–8.42 cal mol−1). The BDE99 shows a higher binding energy than its isomer (BDE100). On the other hand, the lgKow-depth plotting figure shows that a higher Kow value (hydrophobicity) of PBDEs is accompanied by a deeper binding site within the central channel of HSA. This work may provide a theoretical method to assess the transport and distribution of PBDEs in human body.

AB - This work has evaluated the interactions of HSA and typical PBDEs (BDE47, BDE99, BDE100, BDE153 and BDE209) at molecular level by modelling. Apart from the BDE209, PBDEs with higher molecular weight show higher binding energy with the residues of HSA. The BDE209 without H atoms has the lowest binding energy (-ΔGbinding: 4.30 cal mol−1) than other PBDEs (-ΔGbinding: 7.93–8.42 cal mol−1). The BDE99 shows a higher binding energy than its isomer (BDE100). On the other hand, the lgKow-depth plotting figure shows that a higher Kow value (hydrophobicity) of PBDEs is accompanied by a deeper binding site within the central channel of HSA. This work may provide a theoretical method to assess the transport and distribution of PBDEs in human body.

KW - Binding depth

KW - Human serum albumin

KW - Molecule docking

KW - Polybrominated diphenyl ethers

UR - https://www.scopus.com/pages/publications/85021414249

U2 - 10.1016/j.etap.2017.06.005

DO - 10.1016/j.etap.2017.06.005

M3 - 文章

C2 - 28672162

AN - SCOPUS:85021414249

SN - 1382-6689

VL - 54

SP - 34

EP - 39

JO - Environmental Toxicology and Pharmacology

JF - Environmental Toxicology and Pharmacology

ER -

Interaction studies of polybrominated diphenyl ethers (PBDEs) with human serum albumin (HSA): Molecular docking investigations

Abstract

UN SDGs

Keywords

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