The amino acid extends the C-terminal which is tagged onto the VS-9 peptide, a short anti-cancer peptide. Tyrosine, arginine, and lysine have all been noted. The choice of amino acid types at every point stretches reliant on the hydrophobic and hydrophilic residues area, as can be observed in the VS-9 template's helical wheel pattern. The addition of oligopeptide tags should take into account their physiochemical features such as positive net charge, hydrophobicity, and their proportion of hydrophilic amino acids as well as their polar angles. C-terminal NH2- amidation and tyrosine substitutes with arginine or lysine bit enhance the effects against RAW.264.7, hRBCs cells, and human colon cancer test cells. The hydrophobicity (55%), +6 polar positive charges, polar angles (-0.03), and (-0.05) hydrophobicity of the RT2 and CRT2 peptides were effects against four colon cancer cell lines. The morphological assessment revealed good selectivity of RT2 and CRT2 activity in CRC cell lines. Finally, this study found that RT2 and CRT2 unique anti-cancer peptides could potentially be developed in the future for alternative anticancer peptides in clinical applications.