## 3 Results
### Molecular Docking Studies  
Extensive molecular docking studies were performed on all synthesized molecules to elucidate their mechanisms in inhibiting essential functional regions of BSA, to assess their efficacy as anti-inflammatory agents and to provide a detailed analysis of their binding affinities and interaction profiles. This approach enabled a thorough investigation into the specific binding energies and the nature of interactions, shedding light on how these molecules might exert their effects on BSA's functionality. Additionally, Aspirin was docked with the BSA protein to provide a reference for estimating the inhibitory efficacy of the synthesized compounds, allowing for a comparative analysis of their binding interactions and potential effectiveness. The docking modeling results for the top two synthesized molecules, along with the reference ligand (Aspirin), are presented in Table 3, detailing binding affinities and interaction energies. Figure 5 illustrates the specific types of interactions with the BSA active site. The findings reveal that the two leading synthesized compounds, **4d** and **3c**, demonstrate binding affinities of \(-5.274\) kcal.mol\({}^{-1}\) and \(-4.731\) kcal.mol\({}^{-1}\), respectively, indicating stronger interactions with BSA compared to the reference compound (Aspirin), which has a binding affinity of \(-4.641\) kcal.mol\({}^{-1}\). While the docking results suggest stronger interactions of **4d** and **3c** with BSA, only compound **4d** exhibited greater experimental inhibitory activity than Aspirin. These results underscore the importance of correlating in silico predictions with experimental data, as molecular docking does not always directly translate to biological efficacy. The molecule **4d** interacted with amino acids Tyr149 and Arg256 through hydrogen bonding at distances of 2.0 A and 2.1 A, respectively. In addition, the molecule **3c** exhibited a hydrogen bond interaction with Tyr149 and Arg256 at a distance of 2.2 A. The reference ligand formed hydrogen bonds with amino acids Tyr149 and Arg256, with interaction distances ranging from 2.2 to 2.5 A. In addition, a Pi-sulfur interaction was observed involving the sulfur atoms on the thiazole rings of both the **4d** and **3c** molecules. The molecule **4d** showed Pi-sulfur interactions with amino acids Tyr149 and Arg256 at distances ranging from 2.9 to 3.1 A. In contrast, **3c** exhibited a Pi-sulfur \begin{table}
\begin{tabular}{c c c c c} \hline \hline
**Compounds** & **Equations** & **R2** & **K (M\({}^{-1}\))** & \(\Delta\)**G** \\  & & & & **(Kcal.mol\({}^{-1}\))** \\ \hline
**4d** & \(y=-1.220-0.013X\) & 0.979 & \(16.30\times 10^{3}\) & \(-5.75\) \\ \hline
**3c** & \(y=-1.107-0.030X\) & 0.984 & \(5.95\times 10^{3}\) & \(-5.16\) \\ \hline Aspirin & \(y=-1.115-0.016X\) & 0.987 & \(12.40\times 10^{3}\) & \(-5.59\) \\ \hline \hline \end{tabular}
\end{table} 
Table 2: Binding free energies and binding constants for the examimated molecules with the BSA protein via UV–Visible spectroscopy. \begin{table}
\begin{tabular}{c c c c c c c} \hline \hline
**Molecules** & **AG (XP)** & **H-Bond** & **Distance (Å)** & **Pi–sulfur** & **Distance (Å)** & **Hydrophobic** & **Distance (Å)** \\ \hline
**4d** & \(-5.274\) & Tyr149, Arg256 & [2.0–2.1] & Tyr149, & [2.9–3.1] & Tyr149, Leu237, & [3.7–4.8] \\  & & Arg256 & & & & His241, Ile263, & \\  & & & & & & Ile289, Ala290, & \\ \hline
**3c** & \(-4.731\) & Tyr149 & 2.2 & Tyr149 & 2.1 & Tyr149, His241, & \\  & & & & & & Leu237, Leu259, & [4.1–5.0] \\  & & & & & & Ile263, Ile289, & \\  & & & & & & Ala290 & \\ \hline Aspirinref & \(-4.641\) & Tyr149, Arg256 & [2.2–2.5] & - & - & Leu237 and & [4.3–5.2] \\  & & & & & & Ala290 & \\ \hline \hline \end{tabular}
\end{table} 
Table 3: The molecular interactions between the best synthetized molecules and Aspirin with the BSA active site. interaction exclusively with Tyr149 at a distance of 2.1 A.