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

Abstract

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 × 105 M−1 and 6.375 × 105 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.