Multispectroscopic and molecular modeling studies on the interaction of copper-ibuprofenate complex with bovine serum albumin (BSA).

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 ([Cu2(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)4] 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 Kb were calculated and the thermodynamic parameters ∆G°, ∆H° and ∆S° 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 ɑ-helical content of BSA (from 48.56% to 55.71%) and conformational changes of BSA molecules.