Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 983, Issue 1-3, Pages 133-140Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2010.08.042
Keywords
Syringin; Human serum albumin; Fluorescence; Molecular docking; Atomic force microscopy
Categories
Funding
- Science and Technology Project of Shantou [160-2007]
- Shantou University [YR07003]
Ask authors/readers for more resources
The interaction between syringin and HSA has been studied by AFM, molecule modeling, fluorescence, UV-vis, FTIR and CD spectroscopy. Fluorescence results revealed that syringin can enhance the intensity of HSA fluorescence. The enhancement data was analyzed by the equation which developed by Bhattacharya et al. The results showed that there was one primary syringin binding site on HSA with a binding constant of 2.97 x 10(4) M-1 at 295 K. Thermodynamic analysis by Van Hoff equation found enthalpy change (Delta H-0) and entropy change (Delta S-0) were -5.23 kJ mol(-1) and 103.34 J mol(-1) K-1 respectively, which indicated the hydrophobic interaction was the predominant force in the binding process. Competitive experiments showed a displacement of warfarin by syringin, which indicated that the binding site was located at the drug site I. AFM results revealed that the dimension of the individual HSA molecules was larger after interaction with syringin. The secondary structure compositions of free HSA and HSA-syringin complex were estimated by FUR and CD spectra. (C) 2010 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