| This study aims to investigate the interaction between glutathione and bovine serum albumin (BSA)
using ultraviolet–visible (UV–vis) absorption, fluorescence spectroscopies under simulated physiological
conditions (pH 7.4) and molecular docking methods. The results of fluorescence spectroscopy indicated
that the fluorescence intensity of BSA was decreased considerably upon the addition of glutathione
through a static quenching mechanism. The fluorescence quenching obtained was related to the formation
of BSA–glutathione complex. The values of KSV, Ka and Kb for the glutathione and BSA interaction
were in the order of 105. The thermodynamic parameters including enthalpy change (DH), entropy
change (DS) and also Gibb’s free energy (DG) were determined using Van’t Hoff equation. These values
showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of
glutathione to BSA and the stabilization of the complex. Also, the interaction of glutathione and BSA
was spontaneous. The effects of glutathione on the BSA conformation were determined using UV–vis
spectroscopy. Moreover, glutathione was docked in BSA using ArgusLab as a molecular docking program.
It was recognized that glutathione binds within the sub-domain IIA pocket in domain II of BSA. |