کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5507000 | 1536898 | 2017 | 6 صفحه PDF | دانلود رایگان |
- A single state binding mode of Human Serum Albumin with Ellagic Acid is proposed.
- Fluoresence quenching of HSA with Ellagic acid is validated in this study.
- Number of binding sites of HSA is characterized using Molecular Docking and ITC study.
Ellagic acid (EA), a natural polyphenol evidence several pharmacological benefits. The binding profile of EA with human serum albumin (HSA) has been explored and investigated by Isothermal titration calorimetry (ITC), circular dichroism (CD) spectroscopy, time-correlated single-photon counting (TCSPC), absorbance spectroscopy, steady-state fluorescence spectroscopy, and modelling studies. The ITC data analysis revealed the binding Constant (Ka), ÎH, ÎS and ÎG values to be 15.5Ã104Mâ1, â116.2±18.1 Kcal molâ1, â366 cal molâ1Kâ1 and â7.13 Kcal molâ1 respectively with a unique binding site at HSA. EA effectively quenched the intrinsic fluorescence of HSA by static quenching, whereas TCSPC data also revealed association of dynamic quenching also. Thermodynamic analysis confirmed that hydrophobic and mainly hydrogen bonding interaction played important role in stabilizing the HSA-EA complex. It further dictates the binding reaction to be enthalpy driven. The secondary structure of HSA was altered upon binding with EA. CD spectroscopic data indicated the fraction of alpha helicity to be decreased from 52% to 40% upon binding to EA. This study will provide an insight on evaluation of this bioactive interaction during transport and releasing efficiency at the target site in human physiological system since HSA is the most important carrier protein in blood serum.
Journal: Biochemistry and Biophysics Reports - Volume 10, July 2017, Pages 88-93