Fig. 6

Esculetin binds to KEAP1 directly: a 3D Docking model showing esculetin docked to the active site of KEAP1. b 2D interaction diagram of esculetin with KEAP1. Residues involved in hydrogen-bonding, charge or polar interactions are represented by magenta-colored circles. Residues involved in van der Waals interactions are represented by green circles. The solvent accessible surface of a residue is represented by a blue halo around the atom. Hydrogen-bond interactions with amino acid side chain and main chain are represented by a blue and green dashed line, respectively with an arrow head directed toward the electron donor. π-π and π-cationic interactions are represented by an orange line with symbols indicating the interaction. c Western blot analysis of competitive pull down assay carried out with esculetin conjugated beads showing a direct interaction between esculetin and KEAP1. (I stands for input (10 %), B represents protein pulled using non conjugated beads, EB represent protein pulled using esculetin conjugated sepharose beads)