This study evaluated the anticancer potential of peptides from enzymatically hydrolyzed human breast milk on MCF-7 breast cancer cells, focusing on protein expression alterations associated with cell death. Human breast milk was enzymatically hydrolyzed under controlled conditions to simulate gastrointestinal processing, generating bioactive peptides. The hydrolysate was applied to MCF-7 cells for 24 hours, and proteomic changes were characterized using LC-MS/MS-based analysis. Application of the hydrolysate to MCF-7 cells led to notable proteomic alterations, particularly in proteins regulating apoptosis, cell survival, and cancer-related signalling pathways. In silico docking analyses identified three abundant peptides (AGFAGDDAPR, LAADDFR, and DAEAWFNEK) predicted to interact with key regulatory proteins, including myeloid cell leukemia-1, Ras suppressor protein-1, and galectin-3. These peptides showed favorable docking scores, which may indicate their potential involvement in apoptosis- and metastasis-related pathways. Omics-guided evaluation highlights these peptides as promising lead candidates for peptide-based anticancer strategies. This integrative approach demonstrates the utility of combining enzymatic hydrolysis, proteomic profiling, and computational analyses to identify human-derived bioactive molecules with therapeutic potential.
Gökmen et al. (2026) studied this question.