## 3 Results and Discussion
### Molecular Docking Simulation  
Molecular docking simulation is a computational approach used to model interactions between macromolecules and smaller compounds, particularly highlighting the non-covalent biochemical interactions between them. This method enables a detailed visualization and assessment of these molecular interactions, providing valuable insights into potential binding affinities and interaction modes [75]. Additionally, in vitro findings on anti-inflammatory activity can be further correlated with the binding affinities and interaction patterns identified in docking studies. In this study, molecular docking of the SQ compound was conducted to investigate its binding affinity and interaction mode with HSA in order to elucidate its anti-inflammatory properties. HSA contains two primary drug-binding sites, known as Sudlow sites I and II. Docking simulations were performed at these sites using a grid box with the dimensions of 60 \(\times\) 70 \(\times\) 60 A. The results indicated a more favorable binding free energy (\(\Delta\)G) at Sudlow site I compared to Sudlow site II, suggesting a stronger interaction of the SQ compound with Sudlow site I of HSA. Figure 7 shows the binding representation of the synthesized compound with HSA. The amino acid residues of HSA involved in the interaction with the SQ compound are represented as 3D and 2D diagrams in Figure 8. The \(\Delta\)G value for this compound was calculated to be \(-8.18\) kcal/mol, indicating a strong binding affinity. This high affinity suggests that the SQ compound has a significant inhibitory effect on HSA, supporting its potential as an effective inhibitor of this protein.  
Moreover, the docking analysis revealed that the binding interactions between the title compound and HSA are significantly influenced by a combination of hydrogen bonding, van der Waals forces, hydrophobic interactions, and electrostatic attractions. This interplay of forces underscores the complexity and specificity of the binding process, highlighting how each interaction contributes to the stability and affinity of the compound within the HSA binding sites. The SQ compound forms a complex network of interactions with several key amino acid residues of HSA. It establishes two hydrogen bonds with residues LYS 195 and GLU 153, reinforcing stability. Additionally, the compound engages in three electrostatic attractions with LYS 195, GLU 292, and GLU 153, which further stabilize the binding. Hydrophobic interactions are prevalent, with five key connections to ARG 257, HIS 242, VAL 241, and ALA 291. Lastly, four van der Waals forces with residues ILE 290, LEU 260, LEU 238, and SER 192 contribute to the overall structural cohesion of the complex.  
A high degree of interaction between the SQ (**5**) and amino acid residues within HSA plays a crucial role in stabilizing the albumin's structure. These interactions contribute to preserving the integrity of albumin, preventing its denaturation even under inflammatory conditions [76]. The results of this study align well with the observed experimental evidence of the compound's anti-inflammatory effectiveness, affirming its protective role during inflammation.  
Figure 7: The docking perspective of SQ (5) in the interaction with HSA.