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Interaction of human serum albumin with novel imidazole derivatives studied by spectroscopy and molecular docking
Author(s) -
Yue Yuanyuan,
Sun Yangyang,
Dong Qiao,
Liu Ren,
Yan Xuyang,
Zhang Yajie,
Liu Jianming
Publication year - 2016
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3010
Subject(s) - imidazole , human serum albumin , chemistry , circular dichroism , fluorescence , förster resonance energy transfer , docking (animal) , spectroscopy , fluorescence spectroscopy , quenching (fluorescence) , binding constant , acceptor , stereochemistry , binding site , crystallography , photochemistry , chromatography , biochemistry , medicine , physics , nursing , quantum mechanics , condensed matter physics
This study was a detailed characterization of the interaction of a series of imidazole derivatives with a model transport protein, human serum albumin (HSA). Fluorescence and time‐resolved fluorescence results showed the existence of a static quenching mode for the HSA–imidazole derivative interaction. The binding constant at 296 K was in the order of 10 4 M –1 , showing high affinity between the imidazole derivatives and HSA. A site marker competition study combined with molecular docking revealed that the imidazole derivatives bound to subdomain IIA of HSA (Sudlow's site I). Furthermore, the results of synchronous, 3D, Fourier transform infrared, circular dichroism and UV–vis spectroscopy demonstrated that the secondary structure of HSA was altered in the presence of the imidazole derivatives. The specific binding distance, r , between the donor and acceptor was obtained according to fluorescence resonance energy transfer. Copyright © 2015 John Wiley & Sons, Ltd.