| Molecular structural heterogeneity of bisphenols governs their serum albumin binding | |
Zhao, Xingchen; Li, Penghui; Song, Shanjun; Wang, Huiyu; Zhao, Lining; Zong, Wansong; Zhang, Haiyan; Qu, Guangbo; Hu, Ligang; Cai, Zongwei; Jiang, Guibin
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| 2021-08-10 | |
| Source Publication | SCIENCE OF THE TOTAL ENVIRONMENT
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| ISSN | 0048-9697 |
| Volume | 781Pages:- |
| Abstract | Bisphenol A (BPA) and its analogs (bisphenol F, BPF: bisphenol AF, BPAF: bisphenol S, BPS; and tetrabromobisphenol A, TBBPA) are transported by blood and bind estrogen receptors of target organs or cells. They were confirmed to bind human serum albumin (HSA) in blood, and the binding constants of BPA (5.14 x 10(3) M-1), BPF (1.05 x 10(4) M-1). and BPS (7.89 x 10(3) M-1) determined via equilibrium dialysis shows moderate binding ability with multiple binding sites. The HSA-water partition coefficients (log K-HW > 3) are greater than their octanol-water distribution coefficients, and may follow the order: TBBPA > BPAF > BPA (3.75) > BPF (3.61) > BPS (3.27). Functional groups and substitutions of bisphenols (BPs) determine the fluorescence quenching of Trp214 in HSA. The effects follow: TBBPA (4.41 x 10(14) M-1 s(-1)) BPS (4.08 x 10(12) M-1 s(-1)) > BPAF (1.20 x 10(12) M-1 s(-1)) > BPF (3.06 x 10(11) M-1 s(-1)) approximate to BPA (4.47 x 10(11) M-1 s(-1)), which is in line with the molecular docking results. In this process, the enzymatic characteristics of HSA were changed simultaneously, as evidenced by decreased K-m and V-max except for BPS (increased K-m and V-ma(x)) and increased catalytic efficiency, which may improve the hydrolysis of other drugs. However, the native conformation of the protein underwent locally adaptive changes due to the reversible binding. Overall, these data provide a mechanistic explanation for the transport of BPs in human blood, which may affect their retention and toxicity. (C) 2021 Published by Elsevier B.V. |
| Department | 环境化学与生态毒理学国家重点实验室 |
| Keyword | Bisphenots Blood Structural heterogeneity Protein conformation Molecular docking |
| WOS Research Area | Environmental Sciences |
| Document Type | 期刊论文 |
| Identifier | https://ir.rcees.ac.cn/handle/311016/45786 |
| Collection | 环境化学与生态毒理学国家重点实验室 |
| Affiliation | 1.Natl Inst Metrol, Beijing 100029, Peoples R China 2.Tianjin Univ Technol, Tianjin 300384, Peoples R China 3.Chinese Acad Sci, Res Ctr Ecoenvironm Sci, State Key Lab Environm Chem & Ecotoxicol, Beijing 100085, Peoples R China 4.Hebei Univ, Coll Life Sci, Baoding 071000, Peoples R China 5.Shandong Normal Univ, Coll Geog & Environm, Jinan 250014, Peoples R China 6.Univ Chinese Acad Sci, Hangzhou Inst Adv Study, Hangzhou 310024, Peoples R China |
| Recommended Citation GB/T 7714 | Zhao, Xingchen,Li, Penghui,Song, Shanjun,et al. Molecular structural heterogeneity of bisphenols governs their serum albumin binding[J]. SCIENCE OF THE TOTAL ENVIRONMENT,2021,781:-. |
| APA | Zhao, Xingchen.,Li, Penghui.,Song, Shanjun.,Wang, Huiyu.,Zhao, Lining.,...&Jiang, Guibin.(2021).Molecular structural heterogeneity of bisphenols governs their serum albumin binding.SCIENCE OF THE TOTAL ENVIRONMENT,781,-. |
| MLA | Zhao, Xingchen,et al."Molecular structural heterogeneity of bisphenols governs their serum albumin binding".SCIENCE OF THE TOTAL ENVIRONMENT 781(2021):-. |
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| Molecular structural（1768KB） | 期刊论文 | 出版稿 | 开放获取 | CC BY-NC-SA | View Download | |
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