期刊
出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/10934529.2020.1776035
关键词
17 alpha-ethinylestradiol; bovine serum albumin; interaction
资金
- National Natural Science Foundation of China [21676028, 41602351, 31600372]
To understand the effect of 17 alpha-ethinylestradiol (EE2) on the conformation changes of bovine serum albumin (BSA), the binding mechanisms of EE2 with BSA were investigated by fluorescence spectroscopy, time-resolved fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, UV-visible spectroscopy, circular dichroism (CD) spectroscopy and molecular docking. The quenching constants, binding constants, the number of binding sites, thermodynamic parameters, binding distance and the secondary structure changes of BSA were determined. The results of fluorescence quenching experiment suggested that the fluorescence quenching of BSA by EE was due to the formation of complex through static quenching, which was also confirmed by time-resolved fluorescence measurements. The thermodynamic parameters indicated that the binding of EE2 to BSA was driven mainly by van der Waals forces and hydrogen bonding. The conformation alterations of BSA upon EE2 binding were studied by UV-vis spectroscopy and CD spectroscopy. The results of site marker competitive experiments and molecular docking showed that the binding sites of EE2 were mainly located within site I in the subdomain IIA of BSA.
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