A comparative study of binding properties of different coumarin-based compounds with human serum albumin

作者：Yue, Yuanyuan^*; Wang, Zhiyue; Wang, Zhixian; Zhang, Yanyan; Liu, Jianming^*

来源：Journal of Molecular Structure, 2018, 1169: 75-80.

DOI：10.1016/j.molstruc.2018.05.060

• 3-(furan-2-yl)-6-methyl-2H-chromen-2-one
• 6-Chloro-3-(furan-2-yI)-2H-chromen-2-one
• Multispectroscopic techniques
• Docking

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.

• 出版日期2018-10-5
• 单位河南师范大学