Table 7 Summary of docking results
Compound | Binding affinity (kcal/mol) | Inhibition constant (Ki) (nM) | No. of H bond formed | No. of hydrogen bond interaction residues | Distance | Hydrophobic interaction | Residues forming π-interactions |
|---|---|---|---|---|---|---|---|
Quercetin | − 9.7 | 7.76E−08 | 2 | Gln71, Tyr133 | 2.36 and 2.76 | Ser125, An87, Pro88, Leu130, Tyr337, Gly126, Glu202, Val73, Gly120, Gly121 and Asp74 | Trp86, Tyr337 and Asn87 |
Kaempferol | − 8.6 | 4.97E−07 | 1 | Arg296, | 2.30 | Tyr337, Val294, Phe338, Tyr124, Phe295, Phe297, Leu289, Glu292 and Gln291 | Tyr341 and Trp286 |
Ferulic acid | − 7.3 | 4.46E−06 | 3 | His-447, Ser-203 and Glu-202 | 2.59, 1.86 and 2.97 | Gly448, Tyr72, Gly120, Asp74 Gly122, Gly121, Ser125, Tyr124, and Asn87, | Phe338, Phe297, Trp86 and Tyr337 |
Lycopene | − 15.1 | – | 0 | Violated the Lipinski’s rule of five | |||
Leucocyanidin | − 7.8 | 1.92E−06 | 1 | Asp74 | 2.58 | Leu289, Thr75, Phe297, Tyr341, Phe338, Val294, Ser293, Tyr72, and Phe295 | Leu76 and Trp286 |
Gallic acid | − 7.2 | 5.28E−06 | 4 | Trp86, Tyr133, Glu202 and Gly120 | 2.84, 1.92, 2.21 and 2.94 | Gly121, Ser125, Gly126, Ile451, Ser203, Leu130, Tyr 119, Tyr337, His447 and Tyr124 | Trp86 and Gly120 |
Isorhamnetin | − 8.2 | 9.76E−07 | 1 | Gln291 | 2.11 | Tyr337, Phe297, Val294, Ser293, Phe338, Arg296, Phe295, Glu292 and Leu289 | Tyr124, Tyr72, Tyr341, and Trp286 |
Rivastigmine | − 6.9 | 8.75E−06 | 1 | Trp286 | 3.75 | Tyr337,Val294, Phe297,Arg296,Ser293, Phe295, Try124,Phe338, Try341, Try72, Leu289 | Trp286 |