Xanthone and Flavone Derivatives as Dual Agents with Acetylcholinesterase Inhibition and Antioxidant Activity as Potential Anti-Alzheimer Agents

Figure 2

(a) AChE (surface) and docked 14 (blue sticks). (b) AChE active site (surface) bound to 14 (blue sticks). Residues involved in hydrogen interactions (yellow broken line) and π stacking interactions (yellow double arrow) are displayed using a stick model. AChE carbon, oxygen, nitrogen, and hydrogen are represented in green, red, blue, and grey, respectively. (c) 2D depiction of the 14 docked into the binding site of AChE highlighting the protein residues that form the main interactions with the different structural units of the inhibitor. Hydrogen-bonding interactions are represented with yellow broken lines. stacking interactions are represented with a yellow double arrow. Receptor residues that are close to 14, but whose interactions with the ligand are weak or diffuse, such as collective hydrophobic or electrostatic interactions, are also represented (all the ones that have no indication for hydrogen-bonding or π stacking). Hydrophobic residues are colored with a green interior, polar residues are colored in light purple, basic residues are annotated by a blue ring, and acidic residues are annotated with a red ring. Solvent accessible surface area of 14 is plotted directly onto the atoms in the form of a blue smudge.

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