3.5.7. Statistical Analysis

The values of the determined parameters were expressed as mean ± standard deviation (SD). Comparisons were performed by one-way ANOVA followed by a Bonferroni post hoc test for multiple comparisons. Differences at *p* < 005 were considered statistically significant.

#### *3.6. Molecular Modeling Study*

Molecular Operating Environment (MOE) was used to dock both ceramides **A** (**1**) and **B** (**2**) into the transcription factor P53 [90]. First, the crystal structures of P53 (2MEJ) were imported into the MOE graphical interface, and the protein was then prepared for docking using the default parameters of the Protein Preparation module and the Protonate 3D tool. Ligands were also sketched using MOE and minimized with the MMFF94 force field to a gradient of 0.001 kcal/mol·Å2. They were then docked into the putative binding site of the P53 protein using the induced-fit protocol and the default parameters of the MOE Dock module with the Triangle Matcher method. Residues Ser240 and Ser241 were used to specify the binding site as reported in the literature. The default values of 30 docked structures for each ligand were used. Poses were arranged according to the docking scores and inspected visually.
