Table 1.
Total phenolic and flavonoid content, and antioxidant potential of ethanol extract and different fractions of Pueraria tuberosa.
Table 2.
Copper reducing equivalent of ethanol extract and different fractions of Pueraria tuberosa at different concentrations.
Fig 1.
Effect of FRAC from Pueraria tuberosa on biochemical parameters of serum.
Data were average ± SEM (n = 6). *** p < 0.001 significantly different from sham control group. ## p < 0.01, ### p < 0.001 significantly different from OVX group. Ca, calcium; P, phosphorus; ALP, alkaline phosphatase; TRAP, tartrate resistant acid phosphatase; TG, triglycerides; TC, total cholesterol.
Fig 2.
Effect of FRAC from Pueraria tuberosa on biochemical parameters of urine.
Data were average ± SEM (n = 6). *** p < 0.01 significantly different from sham control group. # p < 0.05, ## p < 0.01, ### p < 0.001 significantly different from OVX group. Ca, calcium; P, phosphorus; HP, hydroxyproline.
Fig 3.
Effect of FRAC from Pueraria tuberosa on femur biomechanical parameters.
Data were average ± SEM (n = 6). ** p < 0.01, *** p < 0.001 significantly different from sham control group. # p < 0.05, ## p < 0.01, ### p < 0.001 significantly different from OVX group.
Fig 4.
Effect of FRAC from Pueraria tuberosa on breaking strength of femur and 4th lumbar vertebrae.
Data were average ± SEM (n = 6). *** p < 0.001 significantly different from sham control group. ## p < 0.01, ### p < 0.001 significantly different from OVX group.
Fig 5.
Effect of FRAC from Pueraria tuberosa on body and uterus weight.
Data were average ± SEM (n = 6). *** p < 0.001 significantly different from Sham control group. ## p < 0.01, ### p < 0.001 significantly different from OVX group.
Fig 6.
Effect of FRAC of Pueraria tuberosa on the histopathology of the femur.
A, Photomicrography of the femur of sham control group showing typical bone architecture; B, Photomicrography of the femur of OVX control group showing disruption of trabeculae; C, Photomicrography of the femur of raloxifene treated group showing improved trabecular thickness, and compactness of cells indicating mineralization of bone; D, Photomicrography of the femur of FRAC-100 mg/kg treated group showing the improved trabecular thickness and bone architecture; E, Photomicrography of the femur of FRAC-200 mg/kg treated group showing the restoration of typical bone architecture and an increase in width of trabeculae.
Fig 7.
In vitro cytotoxicity of FRAC of Pueraria tuberosa against different cancer cell lines.
Values are mean ± SEMs (n = 3).
Fig 8.
Docking study of genistein in estrogen receptors.
A, Co-crystalized ligand of 1x76 (genistein) showing hydrogen bond with Arg346, Leu339, and His475. Hydrophobic interactions were also seen near the benzene rings with different amino acid residues of estrogen receptor α (PDB: 1x76). The ligand showed a docking score of -26.1648. B, Co-crystalized ligand of 1x7R (genistein) showing hydrogen bond with Leu346, Arg394, Gly521, Glu353, and His524. Hydrophobic interactions were also seen near the benzene rings with different amino acid residues of estrogen receptor β (PDB: 1x7R). The ligand showed a docking score of -32.4084.
Fig 9.
Docking study of daidzein in estrogen receptors.
A, Docking pose of daidzein in estrogen receptor α (PDB: 1x76) active site with a docking score of -28.3129. Daidzein formed a hydrogen bond with Arg346, Glu305, and His475. Hydrophobic interactions were also seen near the benzene rings with different amino acid residues of estrogen receptor α (PDB: 1x76). B, Docking pose of daidzein in estrogen receptor β (1 x 7R) active site with a docking score of -31.8923. Daidzein showed a hydrogen bond with Arg394, Glu353, Gly521 and His524. Hydrophobic interactions were also seen near the benzene rings with different amino acid residues of estrogen receptor β (PDB: 1x7R).
Fig 10.
Docking study of internal ligands on Ix76 and 1x7R receptors.
A, Docking pose of daidzein in estrogen receptor α (PDB: 1x76) active site with a docking score of -28.3129. Daidzein formed hydrogen bond with Arg346, Glu305, and His475. Hydrophobic interactions were also seen near the benzene rings with different amino acid residues of estrogen receptor α (PDB: 1x76). B, Docking pose of 5-hydroxy-2-(4-hydroxyphenyl)-1-benzofuran-7-carbonitrile in estrogen receptor β (1 x 7R) active site with a docking score of -28.9356. 5-hydroxy-2-(4-hydroxyphenyl)-1-benzofuran-7-carbonitrile showed a hydrogen bond with Arg394, Glu353and His524. Hydrophobic interactions were also seen near the benzene rings with different amino acid residues of estrogen receptor β (PDB: 1x7R).
Table 3.
Details of different drug-likeness rules, bioavailability, lead-likeness, synthetic accessibility, and alerts for PAINS and Brenk.
Table 4.
Details of in-silico ADME profile of flavonoids using Swiss ADME online server.