Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 888, Issue 1-3, Pages 25-32Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2007.11.028
Keywords
Esculetin; Human serum albumin (HSA); Fluorescence polarization (FP); Circular dichroism (CD); Fourier transformation infrared spectra (FT-IR)
Categories
Funding
- National Natural Science Foundation of China [20275014]
Ask authors/readers for more resources
Esculetin derived from Cortex fraxin plays an important role as a traditional Chinese medicine because of its unique pharmacological properties. The interactions between esculetin and HSA were studied by fluorescence spectroscopic techniques under similar to human physiologic conditions. The binding parameters have been evaluated by fluorescence quenching methods. The results proved the mechanism of fluorescence quenching of HSA while interacting with esculetin is due to the formation of esculetin-HSA complex formation. The thermodynamic parameters like Delta H-0 and Delta S-0 were calculated to be - 14.62 kJ/mol and 38.93 J/mol/K, respectively, which proves main interaction between esculetin and HSA is hydrophobic contact, but the electrostatic interaction cannot be excluded, which in agreement with the result of molecular docking study. The distance r between donor (HSA) and acceptor (esculetin) was obtained according to the Forster's theory of non-radiative energy transfer and found to be 2.89 nm. From the high value of fluorescence anisotropy (r = 0.07) it was argued that the probe molecular was located in motionally restricted environment of the protein. The alterations of protein secondary structure in the presence of esculetin were confirmed by the evidences from UV, FT-IR and CD spectroscopes. In addition, the effects of common ions and amino acids on the constants of esculetin-HSA complex were also discussed. (C) 2007 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available