Molecular docking and ADMET studies of the interaction of 4-carboxyl-2,6-dinitrophenylazohydroxynaphthalenes with bovine serum albumin

Previous spectrophotometric investigations revealed strong binding affinities between four potential monoazo colourants (code-named AZ-01 to 04) and bovine serum albumin (BSA) which could dictate the tissue distribution toxicity of additives. The molecular docking interactions dyes with BSA were analyzed using AutoDock vina PatchDock in order elucidate functional groups involved complex stabilization. Docking conformations confirmed ligands preferentially inserted into hydrophobic cavities site I. Structure-BSA relationships AZ-02 was driven by hydrogen bond donation from its free phydroxynaphthalene substituent Ser-479 while predominantly hydrazone form positional isomer, AZ-01, increased lipophilicity tendency for interactions. relatively higher C/H ratio AZ-03 - 04, contain additional C-7 substituents, responsible their stronger extensive involvement aromatic rings ligand-site I stabilization via Pi-Pi T-shaped, Pi-alkyl alkyl-alkyl Moreso, -03 -04 exist as tautomers an overall positive charge provided complementary modes interaction negatively charged aspartic glutamic acids. structure-BSA molecules, can be employed synthesis safer congeners, have been elucidated.