The interaction of 10 synthetic food dyes with human serum albumin (HSA) was investigated using fuorescence spectroscopy, biopartitioning micellar chromatography (BMC) and molecular docking studies. The results obtained by fuorescence spectroscopy indicated that these dyes could strongly quench the intrinsic fuorescence of HSA due to interaction with Trp-214 residue of HSA. The binding constant (Kb) and the number of HSA binding sites were calculated using modifed Stern–Volmer equation. BMC as a micellar mobile phase is used as an in vitro system by polyoxyethylene 23 lauryl ether (Brij-35) to predict the Kb of food dyes to HSA. The relationship between the BMC retention data and Kb of food dyes was modeled and the predictive ability of model evaluated. The correlation coefcient (R) and standard error (SE) of developed model were 0.928 and 1.994, respectively. Moreover, molecular docking explorations show that interaction occurs in the subdomain IIA (site I)
