Scheme 1.
Fig 1.
Optimized structures of quinolone derivatives.
Table 1.
Calculation of energetic parameters and quantum chemical descriptors of quinolone derivatives.
Fig 2.
HOMO and LUMO structures of quinolone derivatives in gas and solvent (water) phase.
Table 2.
Quantum chemical descriptors of quinolone derivatives in gas phase.
Fig 3.
Molecular electrostatic potential (MEP) structures of quinolone derivatives in gas phase and solvent phase as well.
Fig 4.
3D and 2D interactions of Nap (co-crystal ligand) with active site of AKR1B1.
Table 3.
Binding energies of quinolone derivatives with target AKR1B1 and AKR1B10 (kJ/mol).
Fig 5.
3D and 2D interactions of quinidine with active site of AKR1B1.
Fig 6.
3D and 2D interactions of quinine with active site of AKR1B1.
Fig 7.
3D and 2D interactions of Nap (co-crystal ligand) with active site of AKR1B10.
Fig 8.
3D and 2D interactions of quinidine with active site of AKR1B10.
Fig 9.
3D and 2D interactions of quinine with active site of AKR1B10.
Fig 10.
3D and 2D interactions of quinine with active site of nuclear factor kappa B (NF-κB).
Fig 11.
3D and 2D interactions of quinidine with active site of nuclear factor kappa B (NF-κB).
Fig 12.
. 3D and 2D interactions of quinidine with active site of cellular tumor antigen P53.
Fig 13.
3D and 2D interactions of quinine with active site of cellular tumor antigen P53.
Fig 14.
3D and 2D interactions of quinine with active site of caspase-3.
Fig 15.
3D and 2D interactions of quinidine with active site of caspase-3.
Fig 16.
Root mean square deviation (RMSD) of the C-alpha atoms of AKR1B1-Quinine, AKR1B1-Quinidine; AKR1B10-Quinine, AKR1B10-Quinidine complexes with time.
The left Y-axis shows the variation of protein RMSD through time. The right Y-axis shows the variation of ligand RMSD through time.
Fig 17.
Residue wise Root Mean Square Fluctuation (RMSF) of the C-alpha atoms of AKR1B1-Quinine, Quinidine; AKR1B10-Quinine, Quinidine complexes with time.
Fig 18.
AKR1B1, AKR1B10 bound with quinidine secondary structure element distribution by residue index.
The colours red and blue represent alpha helices and beta strands, respectively.
Fig 19.
AKR1B1, AKR1B10 bound with quinine secondary structure element distribution by residue index.
The colours red and blue represent alpha helices and beta strands, respectively.
Table 4.
Physicochemical properties of quinolone derivatives.
Table 5.
ADMET properties of the quinolone derivatives.