Abstract

Bovine serum albumin (BSA) represents the well recognized model protein for investigations of diverse intermolecular reactions in studies on pharmacological activities of modern drugs. In the present work, the interaction between copper ibuprofenate (1Cu2(IBU)4]) and BSA under simulative physiological conditions was investigated by the using of diverse spectral methods including fluorescence, UV-vis absorption, CD spectroscopy and also molecular docking. The obtained results showed that there was a strong fluorescence quenching of BSA by Cu2(IBU)4 (2.964E+4 M-1 at room temperature). Using the continuous variation method, a single class of binding sites, (1:1), for Cu2(IBU)41 on BSA was put in evidence. The Stern-Volmer analysis of fluorescence quenching data shows the presence of the static quenching mechanism. The binding constants K-b were calculated and the thermodynamic parameters Delta G degrees, Delta H degrees and Delta S degrees were given. The obtained thermodynamic values and the change observed in the alpha-helical content signature suggests that hydrogen bonding and hydrophobic forces play a major role in the Cu2(IBU)4]-BSA binding interaction. Site marker competitive experiments indicated that the binding of Cu2(IBU)4 to BSA primarily took place in sub-domain IIA that this observation were substantiated by molecular docking studies. The results of CD and UV-vis spectroscopy showed for the first time that the presence of Cu2(IBU)4 increased the a-helical content of BSA (from 48.56% to 55.71%) and conformational changes of BSA molecules. (C) 2017 Elsevier B.V. All rights reserved.