Molecular Docking and Semi-Empirical Study of the Binding between Allura Red, a synthetic food dye, with Bovine Serum Albumin


Otávio Augusto Chaves, Robson Pacheco Pereira , Molecular Docking Studies of the Binding between Allura Red, a synthetic food dye, with Plasmatic Albumin(2016)SDRP Journal of Food Science & Technology 1(5)


The interaction between Bovine Serum Albumin (BSA), one of the standard proteins used to study the bioavailability of biological molecules in the bloodstream, and allura red, a commercial food additive, was studied by molecular docking. The computational results suggest GoldScore as the main function to study the BSA:Allura red interactions. The most probable binding site to Allura red is the site IIA (Sudlow’s site I), where Trp212 residue can be found and the Student's t-distribution indicate that there are statistically significant differences between the two data sets obtained by molecular docking. The molecular docking results suggest that Allura red interacts with Arg-194, Arg-198, Trp-212, Arg-217, Gln-220, Lys-294 and Ser-343 residues, by different intermolecular interactions (electrostatic forces, hydrogen bonding and hydrophobic interactions). After semi-empirical optimization, the amino acid residues Gln-220 and Lys-294 exhibited a significantly different interaction structure with Allura red. Theoretical interaction enthalpy change value (△Hint=14.0 kJ/mol) reinforces the proposal that the preferential interaction cavity for Allura red in BSA is the Trp-212containing site.


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