期刊
JOURNAL OF MOLECULAR STRUCTURE
卷 1169, 期 -, 页码 75-80出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2018.05.060
关键词
3-(furan-2-yl)-6-methyl-2H-chromen-2-one; 6-Chloro-3-(furan-2-yI)-2H-chromen-2-one; Multispectroscopic techniques; Docking
资金
- National Natural Science Foundation of China [21573057]
- Program for Innovative Research Team in University of Henan Province [17IRTSTHN001]
- Key Scientific Research Project of Higher Education of Henan Province [17A150029]
We have disclosed the impact of different coumarin-based compounds (3-(furan-2-yl)-6-methyl-2H-chromen-2-one (FM) and 6-chloro-3-(furan-2-yl)-2H-chromen-2-one) (CM)) on the change of human serum albumin's structure in vitro. The fluorescence experiments demonstrated that the HSA native fluorescence intensity was more reduced by CM than FM followed a static mode. We found the binding constants for FM and CM are 1.289 x 10(5 )M(-1) and 6375 x 10(5) M-1, respectively, suggesting the much stronger binding affinity of CM to HSA than FM. Thermodynamic analysis showed the hydrophobic interaction between these coumarin-based compounds and HSA were clearly important. Moreover, a series of spectral methods were used to provide more details about the FM/CM-induced conformational changes of HSA. Finally, we used molecular docking set up a new HSA-FM/CM model to predict the possible binding sites. (C) 2018 Elsevier B.V. All rights reserved.
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