## 3 Results
### MD Simulation and Stability  
Molecular dynamics simulations are carried out to comprehensively evaluate the stability and interaction dynamics of the synthesized molecules within the active site of the BSA protein. This involves detailed analyses of their binding affinities, structural stability and atomic-level mobility, which are compared to those of the reference drug (Aspirin) under similar simulation conditions. The study further aims to explore the capability of the synthesized molecules to inhibit the biological function of the BSA protein by assessing their influence on its structural and functional properties. These findings are intended to provide a deeper understanding of the molecules' therapeutic potential and their comparative effectiveness against the reference drug [47; 48; 49]. Table 6 presents an in-depth analysis of the average values for four essential parameters (RMSD, RMSF, Rg and SASA), each serving a unique purpose in assessing the dynamic behavior of the generated complexes. RMSD gauges the overall stability of the structure by quantifying the deviation of atomic positions from the initial conformation, with smaller values signifying greater stability. RMSF measures the flexibility of individual residues or atoms, highlighting regions with considerable conformational variation. Rg provides insights into the compactness of the complex, where lower values indicate a more stable and tightly packed structure. SASA quantifies the degree of exposure of the molecule to the solvent, providing key information on folding and interactions with the surrounding medium. Collectively, these parameters offer a comprehensive assessment of the structural integrity and dynamic behavior of the complexes. \begin{table}
\begin{tabular}{c c c} \hline \hline  & **4d** & **Aspirin** \\ \hline MW (g/mol) & 187.33 & 180.16 \\ Consensus Log Po/w & 2.36 & 1.28 \\ Log S & \(-\)2.77 & \(-\)1.85 \\ Bioavailability & 0.55 & 0.85 \\ GI absorption & High & High \\ Cytochrome P450 inhibition & No & No \\ Lipinski & Yes & Yes \\ Synthetic accessibility & 2.47 & 1.52 \\ \hline \hline \end{tabular}
\end{table} 
Table 4: Pharmacokine and physicochemical parameters determined through SwissADME. \begin{table}
\begin{tabular}{c c c c c c c} \hline \hline  & **Hepatotoxicity** & **Neurotoxicity** & **Cardiotoxicity** & **Carcinogenicity** & **Cytotoxicity** & **LD\({}_{50}\) (mg/kg)** & **Class** \\ \hline
**4d** & Inactive & Inactive & Inactive & Inactive & 960 & 4 \\ \hline \hline \end{tabular}
\end{table} 
Table 5: Toxicity prediction of the top synthesized molecule via the ProTox-II webserver. The RMSD results indicate that the **4d_BSA** complex exhibits superior stability compared to the Aspirin_BSA complex throughout the 300 ns simulation period. The fact that the Aspirin_BSA complex deviates at 30 ns and 70 ns suggests that the complex undergoes structural adjustments or fluctuations before reaching a stable conformation. These deviations could be due to the complex undergoing conformational changes or adjustments to optimize the binding between Aspirin and the BSA protein. In contrast, the **4d_BSA** complex demonstrates exceptional and constant stability throughout the simulation. The absence of significant deviations implies that the synthesized **4d** molecule binds more stably within the active site of the BSA protein, maintaining its structure without undergoing major conformational changes. This may indicate that the **4d** molecule has a stronger or more optimal interaction with BSA compared to Aspirin, contributing to its enhanced stability. The average RMSD values further reinforce these observations. With an average RMSD of 0.18 nm, the **4d_BSA** complex shows a high degree of structural integrity and less fluctuation compared to the Aspirin_BSA complex, which has a higher average RMSD of 0.32 nm. This suggests that **4d** interacts more stably with BSA, potentially offering a more reliable and sustained binding interaction.