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The main aim of this work was to gain insight into the binding properties between a food colorant, citrus red 2 (CR), and human serum albumin (HSA), which is the predominant protein in blood plasma. Here, computer simulations and multiple spectroscopies were applied to predict and characterize the interaction between CR and HSA. Docking and molecular dynamics presented a stable binding configuration with low fluctuations. Fluorescence spectroscopy and lifetime results suggested that the CR–HSA combination undergoes static quenching mechanism with binding constant of 10 5  L/mol. Displacement analysis showed the binding of CR at site I of HSA, which agrees with the docking results. The binding process occured spontaneously and was mainly driven by electrostatic interactions. Synchronous fluorescence and circular dichroism measurements demonstrate the changes in the microenvironment residues and  α -helix contents of HSA induced by CR. The computational and experimental techniques are complementary to clearly understand the food colorant transportation and bioaccumulative toxicity in the human body.

Computational and spectroscopic analysis of interaction between food colorant citrus red 2 and human serum albumin