An insight to the binding of ellagic acid with human serum albumin using spectroscopic and isothermal calorimetry studies.

ABSTRACT: 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), ΔH, ΔS and ΔG values to be 15.5×104M-1, -116.2±18.1 Kcal mol-1, -366 cal mol-1K-1 and -7.13 Kcal mol-1 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 hydrophobi

SUBMITTER: Pattanayak R 

PROVIDER: S-EPMC5637241 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature