Study of interaction of butyl p-hydroxybenzoate with human serum albumin by molecular modeling and multi-spectroscopic method

Study of the interaction between butyl p-hydroxybenzoate (butoben) and human serum albumin (HSA) has been performed by molecular modeling and multi-spectroscopic method The interaction mechanism was predicted through molecular modeling first then the binding parameters were confirmed using a series of spectroscopic methods including fluorescence spectroscopy UV-visible absorbance spectroscopy circular dichroism (CD) spectroscopy and Fourier transform Infrared (FT-IR) spectroscopy The thermodynamic parameters of the reaction standard enthalpy Delta H-0 and entropy Delta S-0 have been calculated to be -29 52 kJ mol(-1) and -24 23J mol(-1) K-1 respectively according to the Van t Hoff equation which suggests the van der Waals force and hydrogen bonds are the predominant intermolecular forces in stabilizing the butoben-HSA complex Results obtained by spectroscopic methods are consistent with that of the molecular modeling study In addition alteration of secondary structure of HSA in the presence of butoben was evaluated using the data obtained from UV-visible absorbance CD and FT-IR spectroscopes (C) 2010 Elsevier B V All rights reserved