MDM2 and breast cancer: Here, every selected top compound exhibited hydrophobic bond interactions with active site residues such as Leu-54, Leu-57, Gly-58, Ile-61, Met-62, Val-93, His-96, and Ile-99, indicating a potential disruption of MDM2-p53 dimerization and suggesting a viable therapeutic strategy for altering the MDM2-p53 interaction in BC treatment.