标题:Toxic interaction mechanism of two fluoroquinolones with serum albumin by spectroscopic and computational methods
作者:Qin, Pengfei; Pan, Xingren; Liu, Rutao; Hu, Changwei; Dong, Yuliang
作者机构:[Qin, Pengfei; Hu, Changwei; Dong, Yuliang] Linyi Univ, Shandong Prov Key Lab Water & Soil Conservat & E, Coll Resources & Environm, Linyi, Shandong, 更多
通讯作者:Qin, Pengfei
通讯作者地址:[Qin, PF]Linyi Univ, Coll Resources & Environm, Linyi 276005, Shandong, Peoples R China.
来源:JOURNAL OF ENVIRONMENTAL SCIENCE AND HEALTH PART B-PESTICIDES FOOD CONTAMINANTS AND AGRICULTURAL WASTES
出版年:2017
卷:52
期:11
页码:833-841
DOI:10.1080/03601234.2017.1356177
关键词:Fluoroquinolones; serum albumin; fluorescence; molecular docking
摘要:To evaluate the toxicity of two fluoroquinolones (FQs), ciprofloxacin (CPFX), and enrofloxacin (ENFX), at the protein level, their binding modes with bovine serum albumin (BSA) were characterized by multiple spectroscopic and molecular docking methods under simulated physiological conditions. On the basis of fluorescence spectra, we concluded that both FQs greatly quenched the fluorescence intensity of BSA, which was attributed to the formation of a moderately strong complex mainly through electrostatic interactions. Besides, CPFX posed more of an affinity threat than ENFX. The molecular docking methods further illustrated that both CPFX and ENFX could bind into the subdomain IIIA of BSA and interact with Arg 508 and Lys 437, the positively charged residues in protein. Furthermore, as shown by the synchronous fluorescence, UV-Visible absorption and circular dichroism data, both CPFX and ENFX could lead to the conformational and microenvironmental changes of BSA, which may affect its physiological function.
收录类别:EI;SCOPUS;SCIE
WOS核心被引频次:1
Scopus被引频次:2
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85029905071&doi=10.1080%2f03601234.2017.1356177&partnerID=40&md5=52f91308c3e94dd2ad09543b21095339
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