Table 2 Protein-ligand interaction assessment of the lead candidates, stigmasterol, and donepezil.
Ligands | Interacting sites | PAS residues | Anionic subsite residues | Catalytic site residues | Hydrogen-bonding residues (Distance in Å) | Number of hydrogen bonds | Hydrophobic-interaction residues | Binding affinity (kcal/mol) |
|---|---|---|---|---|---|---|---|---|
SA4 | Trp286, Leu289, Val294, Phe295, Arg296, Phe297, Tyr337, Tyr341 | Trp286, Tyr341 | Tyr337 | No residue | Phe295(2.14,2.85), Arg296(2.81), Tyr337(2.58) | 4 | Trp286, Leu289, Val294, Phe297, Tyr341 | -10.9 |
SA12 | Trp286, Leu289, Val294, Phe297, Tyr337, Tyr341 | Trp286, Tyr341 | Tyr337 | No residue | Trp286(3.31), Try337(2.63) | 2 | Trp286, Leu289, Val294, Phe297, Tyr341 | -10.6 |
SA15 | Trp286, Leu289, Glu292, Ser293, Val294, Phe297, Tyr337, Tyr341 | Trp286, Tyr341 | Tyr337 | No residue | Glu292(2.09), Ser293(2.73, 3.20), Tyr337(2.27) | 4 | Trp286, Leu289, Val294, Phe297, Tyr341 | -10.5 |
Stigmasterol | Trp286, Leu289, Val294, Phe297, Tyr341 | Trp286, Tyr341 | No residue | No residue | No residue | 0 | Trp286, Leu289, Val294, Phe297, Tyr341 | -9.6 |
Donepezil (control) | Tyr72, Trp286, Ser293, Phe295, Arg296, Tyr337, Phe338, Tyr341 | Tyr72, Trp286, Tyr341 | Tyr337, Phe338 | No residue | Phe295(2.48) | 1 | Tyr72, Trp286, Ser293, Arg296, Tyr337, Phe338, Tyr341 | -8.7 |
