Determination of the dissociation constants for the interaction of cationic anticancer peptides and FPE-labelled melanoma cells

Alterations in the composition of the cancer cell membrane are one of the hallmarks of cell malignancy. The exposure of phosphatidylserine in the outer leaflet of the cancer cell membrane is partially responsible for membrane electrostatic surface potential alterations, more negative regarding normal cells. This difference is convenient to design anticancer cationic peptides, an alternative to traditional cancer treatment. We have investigated the effect of the peptide net charge using a specific binding model with a Hill slope for the interactions between a melanoma cell line (Sk-mel-28) and peptides from the family G(IIKK)nI-NH2 (n= 2-4).