期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 153, 期 -, 页码 688-703出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2015.09.023
关键词
Imidazole derivatives; Human serum albumin; Quenching mechanisms; Molecular modeling
类别
资金
- National Natural Science Foundation of China [21205029]
- National Undergraduates Innovating Experimentation Project [201310476024]
Small molecular drugs that can combine with target proteins specifically, and then block relative signal pathway, finally obtain the purpose of treatment. For this reason, the synthesis of novel imidazole derivatives was described and this study explored the details of imidazole derivatives binding to human serum albumin (HSA). The data of steady-state and time-resolved fluorescence showed that the conjugation of imidazole derivatives with HSA yielded quenching by a static mechanism. Meanwhile, the number of binding sites, the binding constants, and the thermodynamic parameters were also measured; the raw data indicated that imidazole derivatives could spontaneously bind with HSA through hydrophobic interactions and hydrogen bonds which agreed well with the results from the molecular modeling study. Competitive binding experiments confirmed the location of binding. Furthermore, alteration of the secondary structure of HSA in the presence of the imidazole derivatives was tested. (C) 2015 Elsevier B.V. All rights reserved.
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