## 3 Results and Discussion
### In Silico Evaluation Results
#### 3.2.3 Molecular Dynamics (MD)  
Figure 8 presents the results from the molecular dynamics (MD) simulations, showcasing the Root-Mean-Square Deviation (RMSD) between the GA3 Ox2 receptor and the ligands GA3 and FCF (Figure 8a). Additionally, the figure illustrates hydrogen bond interactions (Figure 8b), Root-Mean-Square Fluctuation (RMSF; Figure 8c), and the Radius of Gyration (Rg; Figure 8d).  
MD simulations confirmed the stability of the interaction between the GA3 Ox2 receptor and the ligands GA3 and FCF. The RMSD values for both receptor-ligand complexes remained under 1 nm, indicating the strong affinity and stability of the interactions over time. Additionally, four hydrogen bonds for FCF and seven for GA3 were observed, providing notable stability at the binding site for both ligands. The RMSF analysis, which evaluates the motion of protein chain atoms, indicated that the region with the highest fluctuation corresponds to FCF, while GA3 exhibited more consistent behavior. The Rg values (Figure 8d) show a minimal variation of 0.04 nm, with ranges from 2.0 to 2.04 nm for GA3 and 2.09 to 2.13 nm for FCF, further confirming structural stability relative to the center of mass.  
Figure 9 displays the MD simulation results for the auxin receptor (IAA7). The RMSD between the IAA7 receptor and the ligands IAA and FCF is shown in Figure 9a, hydrogen bond interactions in Figure 9b, RMSF in Figure 9c, and Rg in Figure 9d.  
Figure 8: Molecular dynamics results for GA3 Ox2 and gibberellic acid GA3 (endogenous ligand, black line) and FCF (blue line); (**a**) RMSD, (**b**) Hydrogen bonds, (**c**) RMS fluctuation, and (**d**) Radius of gyration.  
RMSD analysis between the IAA7 receptor and the ligands (IAA and FCF) suggests comparable stability over time, indicating that FCF binds similarly to IAA. A maximum of four hydrogen bonds for FCF and three for IAA were observed, which aids in stabilizing the docking (Figure 9b). The RMSF results show that the regions of fluctuation for both FCF and IAA are similar. The Rg values indicate a variation of 0.5 nm (ranging from 0.7 to 1.2 nm) for both ligands, further confirming structural stability during the simulation period.  
FCF is a synthetic plant growth regulator, and although it is known that it plays this role in plants, it is not known how it interacts with them. On the other hand, natural phytohormones such as gibberellin 3A (GA3) and indole acetic acid (IAA) are known to play an important role in plant cell development and growth, acting together to achieve plant development. Therefore, it is interesting to investigate whether other molecules can stimulate these receptors and have positive impacts.  
DM studies simulate the basic environmental conditions in a living system; in this case a solvation box was used containing water and ions, specifically 0.15 M KCl and 0.15 M NaCl, plus the protein (GA3 Ox2 or IAA7), and the ligand (GA3, IAA or FCF). The entire system was run at room temperature (298.15 Kelvin grades).  
In this study, the binding of FCF to both receptors (GA3 Ox2 and IAA7) was evaluated, and we found that FCF has a greater stability over time when bound to gibberellin receptors; this implies that FCF is recognized by GA3 Ox2 receptors and remains bound to them. This suggests that FCF, although not a natural phytohormone, can stimulate GA3 Ox2 receptors and act as a gibberellin agonist, promoting similar effects such as cell elongation.  
To determine the responses in the plant, an in vitro assay was carried out using lettuce, where the germination and elongation of the stem cells were evaluated. This trial allowed  
Figure 9: Molecular dynamics results for IAA7 and IAA (endogenous ligand, black line) and FCF (blue line); (**a**) RMSD LIG after alignment to the backbone, (**b**) hydrogen bonds, (**c**) RMS fluctuation, and (**d**) radius of gyration.  
us to observe that germination and stem cell elongation increase when FCF-doped Hap treatments are used.