期刊
JOURNAL OF MOLECULAR LIQUIDS
卷 258, 期 -, 页码 155-162出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molliq.2018.03.010
关键词
Nisoldipine; Human serum albumin; Fluorescence; Electrochemical methods; Molecular docking
资金
- National Natural Science Foundation of China [21273065]
- Foundation of Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education of China), Wuhan University [ACBM2016002]
Nisoldipine represents a compound with diverse pharmacological activities. The interaction between nisoldipine and human serum albumin (HSA) was investigated using various methods, including UV-vis, three-dimensional fluorescence, synchronous fluorescence, electrochemical methods and molecular docking. The decreased quenching constant upon increasing temperatures and UV-vis absorption difference spectrum revealed that there was a static quenching mechanism rather than a dynamic quenching mechanism in the interaction of nisoldipine with human serum albumin. The thermodynamic parameters demonstrated that the binding of nisoldipine to human serum albumin was spontaneous and hydrogen bonding, hydrophobic interactions as well as electrostatic interactions played major roles in the binding process. The binding distance was 2.31 nm, indicating the presence of fluorescence energy transfer. Site marker competitive experiments and molecular docking demonstrated that the binding site of nisoldipine in human serum albumin was site I (subdomain IIA). In addition, three-dimensional fluorescence as well as synchronous fluorescence spectra suggested conformational changes of HSA due to the interaction with nisoldipine. (C) 2018 Elsevier B.V. All rights reserved.
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