The interaction of human serum albumin with Ethyl 2- [2- (dimethylamino) -4- (4-nitrophenyl) - 1, 3-thiazole-5-yl] -2-oxoacetate was investigated by using isothermal titration UV-visible spectrophotometry in tris-buffer, pH 7.4. According to these results, it was found that there are a set of 4 binding sites for this ligand on HSA with positive cooperativity in the binding process. This thiazole derivative can denature the protein as surfactants. Also, their binding was investigated by molecular dynamics simulation in combination with molecular docking. Parameters of surface area, radius of gyration, hydrogen bonding, RMSD, potential of mean force, diffusion coefficient, radial distribution function, helix and coil structures were obtained. It was observed that surfactant reduce intermolecular hydrogen bond and unfold HSA structure more at higher temperature.