The study of the p53 protein and its interactions with other proteins is key to understanding the mechanisms by which p53 affects tumorigenesis. Mutations in the TP53 gene, which occur in approximately 50% of human cancers, often disrupt its function, highlighting its key role in tumorigenesis. Although structurally challenging due to the presence of unstructured regions, p53 has a well-documented role in DNA damage signaling and cancer progression. In this study, the interaction between p53 and 14-3-3γ monomers was studied using in silico methods. Using tertiary structure modeling, molecular dynamics, molecular docking, and virtual ligand screening, we identified small molecule compounds that can modulate the interaction of p53 with 14-3-3γ. Key findings of the study include identification of a ligand binding pocket in the p53-14-3-3γ interaction interface, generation of full-length models of 14-3-3γ and p53 using in silico methods, and selection of potential protein-protein modulators with high affinity for the proteins under study.