Table 1.
List of phytochemicals selected from B. vulgaris for docking against AChE.
Fig 1.
Structures of phytochemicals of B. vulgaris a) Ascorbic acid b) Niacin c) Pyridoxine d) Folic acid e) Gallic acid f) Catechol g) p-coumaric acid h) Ferulic acid.
Fig 2.
Structures of phytochemicals of B. vulgaris a) o-coumaric acid b) Cinnamic acid c) Myricetin d) Naringenin e) Kaempferol f) Apigenin g) Betanin h) Glycine betaine.
Table 2.
Results of phytochemicals examined for Lipinski rule.
Fig 3.
a) Enzyme ligand interactions within the binding domain of AChE for folic acid (FA) and myricetin (MC) b) Enzyme ligand interactions within the active binding domain of AChE for betanin (BE) and donepezil (DP).
Table 3.
Interaction details of phytochemicals in the proposed site of AChE enzyme.
Fig 4.
Percentage inhibition of AChE activity from 12.5–400 μM concentration of betanin, glycine betaine and the reference standard drug, donepezil.
Results are presented as mean ± SEM for experimental triplicates ****P < 0.0001; **P = 0.0014.
Fig 5.
Percentage inhibition of AChE activity at 100 μM concentration of betanin, glycine betaine and the reference standard drug, donepezil.
Results are presented as mean ± SEM for experimental triplicates.
Fig 6.
a) Dose response analysis of betanin was performed using serial dilutions (12.5 μM– 400 μM). Nonlinear regression analysis depicted 19.34 μM concentration as IC50. b) Dose response analysis of glycine betaine was performed using serial dilutions (12.5 μM– 400 μM). Nonlinear regression analysis depicted 16.41 μM concentration as IC50.
Fig 7.
Dose response analysis of standard reference donepezil was performed using serial dilutions (12.5 μM– 400 μM).
Nonlinear regression analysis depicted 14.27 μM concentration as IC50.
Fig 8.
MD simulation interaction diagrams of 20 ns trajectory showing RMSD plot for complex acetyl cholinesterase- Betanin (A), acetyl cholinesterase- Betaine (B), acetyl cholinesterase- Myricetin (C) and acetyl cholinesterase-Donepezil (D) respectively.
Fig 9.
Protein Root Mean Square Fluctuation (RMSF) plots (Angstrom).
(A) RMSF trajectory plot of acetyl cholinesterase- Betanine complex showing residue-wise fluctuation, (B) RMSF trajectory plot for acetyl cholinesterase- Betaine complex showing residue-wise fluctuation, (C) RMSF trajectory plot of acetyl cholinesterase with Myricetin complex showing residue-wise fluctuation, (D) RMSF trajectory plot of acetyl cholinesterase with Donepezil complex showing residue-wise fluctuation.
Fig 10.
Histogram (stacked bar chart) showing forming H-bonds interactions (green color), hydrophobic interactions (gray violet color), and water bridges (blue color) during 50 ns simulation for complex acetyl cholinesterase-Betanin (A), acetyl cholinesterase- Betaine (B), acetyl cholinesterase- Myricetin (C) and acetyl cholinesterase-Donepezil (D).
Fig 11.
The time frame evolution against the radius of gyration (Rg) (A, C, E and G) displayed on left and the SASA plots of docked complexes over 50 ns MD simulation (B, D, F and H) displayed on right.
Table 4.
IC50 values of phytochemicals along with reference standard in AChE inhibitory assays.