Exploring the interaction between rotenone and human serum albumin

被引:17
作者
Fan, Xiao-Yang [1 ,2 ]
Zhang, Yue [1 ,2 ]
Wang, Jia [1 ,2 ]
Yang, Li-Yun [1 ,2 ]
Jiang, Feng-Lei [1 ,2 ]
Liu, Yi [1 ,2 ]
机构
[1] Wuhan Univ, Coll Chem & Mol Sci, State Key Lab Virol, Wuhan 430072, Peoples R China
[2] Wuhan Univ, Coll Chem & Mol Sci, Key Lab Analyt Chem Biol & Med MOE, Wuhan 430072, Peoples R China
基金
中国国家自然科学基金;
关键词
Rotenone; Human serum albumin; Fluorescence; CD; Molecule docking; MITOCHONDRIA; APOPTOSIS;
D O I
10.1016/j.jct.2013.10.021
中图分类号
O414.1 [热力学];
学科分类号
070201 [理论物理];
摘要
Investigation of interaction between rotenone (Rot) and human serum albumin (HSA) is provided. Fluorescence, UV-visible absorption, circular dichroism (CD), and molecular docking methods have been utilized to study the interaction. The static fluorescence quenching was observed and the binding site of Rot-HSA was shown near the warfarin site. The association for Rot and HSA was spontaneous process driven by enthalpy and the dominant driving force was hydrogen bonding interaction. The result was accordant with the molecular docking result. Furthermore, the microenvironment of tyrosine residue was influenced by the binding of rotenone via the synchronous fluorescence spectra. However, Rot had little effect on the conformation of HSA, which supported by the CD method and 3D-fluorescence spectra. Taking all of results into consideration, we conclude Rot changes the conformation of HSA slightly. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:186 / 192
页数:7
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