Molecular structural heterogeneity of bisphenols governs their serum albumin binding
文献类型：期刊论文
| 作者 | Zhao, Xingchen; Li, Penghui; Song, Shanjun; Wang, Huiyu; Zhao, Lining; Zong, Wansong; Zhang, Haiyan; Qu, Guangbo; Hu, Ligang; Cai, Zongwei |
| 刊名 | SCIENCE OF THE TOTAL ENVIRONMENT
 |
| 出版日期 | 2021-08-10 |
| 卷号 | 781页码:- |
| 关键词 | Bisphenots Blood Structural heterogeneity Protein conformation Molecular docking |
| ISSN号 | 0048-9697 |
| 英文摘要 | 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. |
| WOS研究方向 | Environmental Sciences |
| 源URL | [http://ir.rcees.ac.cn/handle/311016/45786]  |
| 专题 | 生态环境研究中心_环境化学与生态毒理学国家重点实验室 |
| 作者单位 | 1.Shandong Normal Univ, Coll Geog & Environm, Jinan 250014, Peoples R China 2.Natl Inst Metrol, Beijing 100029, Peoples R China 3.Tianjin Univ Technol, Tianjin 300384, Peoples R China 4.Chinese Acad Sci, Res Ctr Ecoenvironm Sci, State Key Lab Environm Chem & Ecotoxicol, Beijing 100085, Peoples R China 5.Hebei Univ, Coll Life Sci, Baoding 071000, Peoples R China 6.Univ Chinese Acad Sci, Hangzhou Inst Adv Study, Hangzhou 310024, Peoples R China |
| 推荐引用方式 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):-. |
入库方式： OAI收割
来源：生态环境研究中心
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