In this work the stability parameters of bovine beta-lactoglobulin, variant A, (BLG-A), with regard to their transition curves induced by cetylpyridinium chloride (CPC), dodecyltrimethylammonium bromide (C12TAB), tetradecyltrimethylammonium bromide (C14TAB), hexadecyltrimethylammonium bromide (C16TAB) and sodium dodecylbenzenesulfonate (SDBS) as ionic surfactants, were determined at 298 K. For each transition curve, the conventional method of analysis which assumes a linear concentration dependence of the pre- and post-transition base lines, gave the most realistic values for ?GD(H2O). Subsequently, the retinol binding was investigated by BLG in the presence of various amounts of these surfactants as its extrinsic functional binding fluorophore. The comparison of the results allowed for determining the binding of retinol by BLG in the presence of these ionic surfactants. Also, the interaction of resveratrol, as a natural polyphenolic compound, bisdemethoxycurcumin (BDMC) and diacetylbisdemethoxycurcumin (DABC) as the bioactive constituents of turmeric with BLG, was studied using molecular docking and molecular dynamics simulation methods. Molecular docking studies revealed that the resveratrol, BDMC and DABC were bound to the surface of the protein by two, four and five hydrogen bond interactions, respectively. Furthermore, the results of molecular dynamics simulation represented that complexation of BDMC to BLG will change the conformation of BLG.
