A fascinating method for predicting the major list mode of a ligand with a target protein with a known three-dimensional structure is molecular docking. It’s a crucial tool in the design of structure-based, computer-supported medicine. The intended benzimidazole derivations bind successfully with the target protein’s active site Voltage-gated Sodium Channel (NavMs)- 5HVX by using Autodock software. The designed emulsion A4, A6, A8 shows good list via hydrophobic and hydrogen bonds, respectively, to the target protein, whereas A1, A2, A3, A5, A7shows hydrophobic cling. The relations introduced by the active derivations within 5 Å compass to the list point of sodium channels and via a GABAergic pathway. In this exploration; all composites are active and A6 and A7 is the most active emulsion with minimal list affinity are named as potent impediments. Hydrophobic commerce of A8 and A7 with LEU168; LEU168; PHE142; LEU168; LEU138; MET175; PHE142; PHE172; LEU168; LEU138 a distinct group. The hydrogen bond conformation between the motes PHE and LEU is another factor is completely honored as indicated which have observed Tables 2 and 3. Docking investigations showed that the planned emulsion and target protein were the list mode of the most active composites. 2D and 3D Structure of designed benzimidazole derivations of A6; A7 and A8 are given (Figures 2, 3, 4).

Figure 1:
Designed benzimidazole derivatives

Figure 2:
2D and 3D Structure Designed Benzimidazole derivatives of A6

Comp. Molecular weight (g/mol) CMC rule violation Lipinski’s rule violation MolLog P H bond donor H bond acceptor No. of Rotatable bonds TPSA (Å2) A1 432.86 g/mol 0 Yes 2.95 1 4 6 83.55 Å2 A2 412.44 g/mol 0 Yes 2.68 1 4 6 83.55 Å2 A3 443.41g/mol 0 Yes 2.40 1 6 7 129.37 Å2 A4 426.46 g/mol 0 Yes 2.88 1 4 7 83.55 Å2 A5 477.31 g/mol 0 Yes 3.05 1 4 6 83.55 Å2 A6 449.48 g/mol 0 Yes 3.15 1 4 6 83.55 Å2 A7 428.44g/mol 0 Yes 2.15 1 5 7 92.78 Å2 A8 398.41g/mol 0 Yes 2.47 1 4 6 83.55 Å2 A9 416.40g/mol 0 Yes 2.84 1 5 6 83.55 Å2 A10 423.42 g/mol 0 Yes 1.81 1 5 6 107.34 Å2 Table 2:
Druglikeness analysis of derivatives of designed compound of benzimidazole

Figure 3:
2 D and 3 D Structure Designed Benzimidazole derivatives of A7

Active Amino acid Bond length Bond Type Bond Category Ligand Energy Docking score A1 LEU168 3.36354 Hydrogen Bond Carbon Hydrogen Bond 22.9420 kcal/mol -8.1 LEU168 3.55906 Hydrophobic Pi-Sigma     LEU168 3.86165 Hydrophobic Pi-Sigma     PHE142 3.80812 Hydrophobic Pi-Pi Stacked     PHE172 4.06452 Hydrophobic Pi-Pi Stacked     LEU138 5.32262 Hydrophobic Pi-Alkyl     A2 THR139 2.49397 Hydrogen Bond ConventionalHydrogen Bond 34.4955 kcal/mol -7.8 LEU168 3.42119 Hydrophobic Pi-Sigma     PHE172 4.16443 Hydrophobic Pi-Pi Stacked     PHE172 4.26798 Hydrophobic Pi-Pi Stacked     PHE142 4.96145 Hydrophobic Pi-Pi T-shaped     ALA135 4.3971 Hydrophobic Alkyl     LEU138 4.32799 Hydrophobic Alkyl     TYR143 5.25675 Hydrophobic Pi-Alkyl     LEU138 5.3909 Hydrophobic Pi-Alkyl     A3 LEU168 3.79525 Hydrogen Bond Carbon Hydrogen Bond 21.0582 kcal/mol -8.3 THR139 3.50541 Hydrogen Bond Carbon Hydrogen Bond     LEU168 3.81015 Hydrophobic Pi-Sigma     LEU168 3.58694 Hydrophobic Pi-Sigma     PHE172 4.16592 Hydrophobic Pi-Pi Stacked     PHE172 4.2107 Hydrophobic Pi-Pi Stacked     UNL1 4.87253 Hydrophobic Pi-Pi Stacked     PHE142 4.77548 Hydrophobic Pi-Pi T-shaped     LEU168 4.94469 Hydrophobic Alkyl     LEU138 5.35849 Hydrophobic Pi-Alkyl     A4 THR139 2.32321 Hydrogen Bond ConventionalHydrogen Bond 20.5745 kcal/mol -7.9 LEU168 3.5664 Hydrophobic Pi-Sigma     PHE172 4.09765 Hydrophobic Pi-Pi Stacked     PHE172 4.33962 Hydrophobic Pi-Pi Stacked     UNL1 4.26071 Hydrophobic Pi-Pi Stacked     PHE142 4.83269 Hydrophobic Pi-Pi T-shaped     LEU138 5.26085 Hydrophobic Pi-Alkyl     A5 THR139 2.27351 Hydrogen Bond ConventionalHydrogen Bond 15.7829 kcal/mol -8.5 LEU168 3.76897 Hydrogen Bond Carbon Hydrogen Bond     LEU168 3.48472 Hydrophobic Pi-Sigma     PHE142 5.76341 Hydrophobic Pi-Pi Stacked     PHE172 4.31901 Hydrophobic Pi-Pi Stacked     PHE172 4.18386 Hydrophobic Pi-Pi Stacked     PHE142 5.27218 Hydrophobic Pi-Pi T-shaped     A6 LEU168 3.94059 Hydrophobic Pi-Sigma 23.7210 kcal/mol -8.1 LEU168 3.58577 Hydrophobic Pi-Sigma     PHE142 3.75521 Hydrophobic Pi-Pi Stacked     LEU168 5.38106 Hydrophobic Alkyl     LEU138 4.31334 Hydrophobic Alkyl     MET175 4.66181 Hydrophobic Alkyl     PHE142 4.45107 Hydrophobic Pi-Alkyl     PHE172 5.21336 Hydrophobic Pi-Alkyl     LEU168 4.04581 Hydrophobic Pi-Alkyl     LEU138 5.41196 Hydrophobic Pi-Alkyl     A7 THR139 2.27153 Hydrogen Bond ConventionalHydrogen Bond 26.7202 kcal/mol -8.7 LEU168 3.7803 Hydrogen Bond Carbon Hydrogen Bond     THR139 3.48539 Hydrogen Bond Carbon Hydrogen Bond     ALA135 3.35577 Hydrogen Bond Carbon Hydrogen Bond     UNL1 3.72372 Hydrogen Bond Carbon Hydrogen Bond     LEU168 3.81841 Hydrophobic Pi-Sigma     LEU168 3.59081 Hydrophobic Pi-Sigma     PHE172 4.22858 Hydrophobic Pi-Pi Stacked     PHE172 4.19296 Hydrophobic Pi-Pi Stacked     UNL1 4.84604 Hydrophobic Pi-Pi Stacked     LEU168 4.96597 Hydrophobic Alkyl     LEU168 4.92852 Hydrophobic Alkyl     LEU138 4.06661 Hydrophobic Alkyl     A8 THR139 2.30219 Hydrogen Bond ConventionalHydrogen Bond 44.7859 kcal/mol -7.8 THR13 3.5655 Hydrogen Bond Carbon Hydrogen Bond     ALA135 3.34208 Hydrogen Bond Carbon Hydrogen Bond     LEU168 3.80109 Hydrophobic Pi-Sigma     LEU168 3.60123 Hydrophobic Pi-Sigma     PHE172 4.25657 Hydrophobic Pi-Pi Stacked     PHE172 4.21428 Hydrophobic Pi-Pi Stacked     UNL1 4.90046 Hydrophobic Pi-Pi Stacked     LEU168 4.98171 Hydrophobic Alkyl     LEU168 4.89463 Hydrophobic Alkyl     LEU138 4.06486 Hydrophobic Alkyl     Table 3:
The active amino residues, bond length, bond category, bond type, ligand energies, and docking scores of benzimidazole

Figure 4:
2D and 3D Structure Designed Benzimidazole derivatives of A8