## 3 Results
### Molecular Docking Analysis  
The molecular docking studies of quercetin, isoquerectin, and genistein were performed against the crystal structure of PPAR\(\alpha\) (PDB 2P54) and PPAR\(\gamma\) (PDB 6 TSG), respectively), mPGES-1 (PDB 4 YL1), prostaglandin H (2) Synthase-1 (PDB 1Q4G), protein kinase CK2\(\alpha\) (PDB 6 TGU), inhibitor-bound human 5-lipoxygenase-activating protein (PDB 2Q7M), and the crystal structure of mPGES-1 bound to inhibitor (PDB 5T36) to determine their binding affinities. The results are synthesized in Table 2 and Figure 6.  
Figure 5: Assessment of knee perimeter throughout the experimental period. Symbols are colored according to their respective experimental group. Differences between the sham, OA, OA_Ptl100, OA_Ptl300, and OA_Al groups were assessed using a two-way ANOVA. Results are expressed as mean \(\pm\) SEM. * \(p\) < 0.05 \(n\)SHAM = 4; \(n\)OA = 4; \(n\)OA_PTL100 = 5; \(n\)OA_PTL300 = 5; \(n\)OA_AI = 5) (SHAM—control animals that underwent all surgical procedures but were not induced OA; OA—osteoarthritic animals; OA_PTL100—osteoarthritic animals that from week two were treated with a concentration of 100 mg/kg of _Pterospartum tridentatum_ extract; OA_PTL300—osteoarthritic animals that from week two were treated with a concentration of 300 mg/kg of _Pterspartum tridentatum_ extract; OA_AI—osteoarthritic animals that from week two were treated with a commercial nonsteroidal anti-inflammatory drug).  
\begin{table}
\begin{tabular}{c c c c c} \hline
**Protein** & **Compound** & \begin{tabular}{c} **Binding Energy** \\ **(kcal/mol)** \\ \end{tabular} & \
\begin{tabular}{c} **Inhibition Konstant** \\ **(\mu M)** \\ \end{tabular} &
\begin{tabular}{c} **Intermolecular Energy** \\ **(kcal/mol)** \\ \end{tabular} \\ \hline PPAR\({}^{\prime}\) & Isoquercetin & \(-7.24\) & \(4.91\) & \(-10.82\) \\ (PDB 6 tsg) & Quercetin & \(-6.23\) & \(26.93\) & \(-10.11\) \\  & Genistein & \(-5.81\) & \(55.18\) & \(-9.09\) \\ COX-2 & Isoquercetin & \(-4.66\) & \(385.08\) & \(-8.24\) \\ (PDB 4 yl1) & Quercetin & \(-4.79\) & \(310.18\) & \(-8.66\) \\  & Genistein & \(-4\) & \(1160\) & \(-7.28\) \\ COX-1 & Isoquercetin & \(-5.98\) & \(41.07\) & \(-9.56\) \\ (PDB 1q4g) & Quercetin & \(-9.01\) & \(0.24772\) & \(-10.80\) \\  & Genistein & \(-8.78\) & \(0.36957\) & \(-9.97\) \\ PPAR\({}^{\alpha}\) & Isoquercetin & \(-7.27\) & \(4.68\) & \(-10.85\) \\ (PDB 2p54) & Quercetin & \(-5.66\) & \(71.17\) & \(-9.54\) \\  & Genistein & \(-6.24\) & \(26.76\) & \(-9.52\) \\ CK2\({}^{\alpha}\) & Isoquercetin & \(-8.66\) & \(0.44756\) & \(-12.08\) \\ (PDB 6 tgu) & Quercetin & \(-9.97\) & \(0.04941\) & \(-11.76\) \\  & Genistein & \(-9.78\) & \(0.06758\) & \(-10.98\) \\
5-LO & Isoquercetin & \(-7.96\) & \(1.46\) & \(-11.54\) \\ (PDB 2q7m) & Quercetin & \(-6.92\) & \(8.43\) & \(-10.80\) \\  & Genistein & \(-6.87\) & \(9.19\) & \(-10.15\) \\ mPGES-1 & Isoquercetin & \(-4.62\) & \(410.41\) & \(-8.2\) \\ (PDB 5t36) & Quercetin & \(-1.52\) & \(5457\) & \(-5.6\) \\  & Genistein & \(-5.04\) & \(201.89\) & \(-8.32\) \\ \hline \end{tabular}
\end{table}
Table 2: Molecular docking results of isoquercetin, genistein, and quercetin against crystal structure of peroxisome proliferatorator-activated receptor alpha and gamma (PPAR\(\alpha\) (PDB 2P54) and PPAR\({}^{\prime}\)(PDB 6 TSG), respectively), mPGES-1 (PDB 4 YL1), prostaglandin H (2) Synthase-1 (PDB 1Q4G), protein kinase CK2\(\alpha\) (PDB 6 TGU), inhibitor-bound human 5-lipoxygenase-activating protein (PDB 2Q7M), and the crystal structure of mPGES-1 bound to inhibitor (PDB 5T36).  
Figure 6: _Cont._  
Isoquercetin demonstrated strong molecular interactions with PPARy, PPARa, CK2a, and 5-LO proteins (binding energies of \(-\)7.24, \(-\)7.27, \(-\)8.66, and \(-\)7.96 kcal/mol, respectively). Genistein and quercetin had docking for CK2a (binding energies of \(-\)9.97 and \(-\)9.78, respectively) and COX-1 (binding energies of \(-\)9.01 and \(-\)8.78, respectively).