Mo-CBP3-PepIII Changes the Proteomic Profile of Gastric Cancer Cells, Induces Membrane Pore Formation, and ROS Overaccumulation

Synthetic peptides have gained prominence due to their potential structural alterations and selective toxicity. In this context, Mo-CBP3-PepIII, derived from Moringa oleifera, was developed to increase selectivity against tumor cells. This study evaluated its activity in AGS cells and demonstrated low toxicity in non-tumor cells, MNP-01. Its mechanism of action was investigated using membrane integrity analyses, reactive oxygen species accumulation, morphological alterations assessed by scanning electron microscopy, and proteomics. The results indicate increases of 2.5-, 2.8-, and 1.5-fold, respectively, in membrane permeability, pore formation, and ROS accumulation in peptide-treated cells compared to controls. Scanning electron microscopy revealed that Mo-CBP3-PepIII-treated cells were severely damaged compared with control cells. Additionally, proteomic analysis identified 3052 proteins in control cells (1970) and treated cells (1532). A deeper look into differentially accumulated proteins revealed that Mo-CBP3-PepII interfere in the accumulation of proteins required for cancer cell growth, development and maintenance, drug resistance. Therefore, future studies should delve deeper into its effects on apoptosis, migration, and tumor invasion, examine the cell signaling pathways involved, and explore the proteins identified in this study to understand their functions in tumor biology and the possible interactions of Mo-CBP3-PepIII with conventional drugs.