Electrical potentiation of the membrane permeabilization by new peptides with anticancer properties.

New polycationic peptides were designed on the basis of 16-mer and 14-mer fragments of the peptide BTM-P1, derived from the Cry11Bb protoxin. The peptides caused mitochondrial, but not red blood cell membrane permeabilization. Conjugation of the cell penetrating hepta-arginine vector to their N- or C-termini through two glycine residues resulted in more active peptides, which also permeabilized the red blood cells with a relatively high plasma membrane potential generated in the presence of valinomycin. The efficiency of the peptides was remarkably higher in the lower ionic strength media. The capability of the plasma membrane permeabilization of the normal red blood cells by the designed conjugated peptides and by known anticancer peptide R7-KLA was also strongly potentiated by the external electrical pulses applied to the cell suspension. These results open the new avenues of the local destruction of solid tumors using the combined "peptide--electrical pulses" synergistic treatment. The designed peptides were active against the human leukemia Jurkat cells but not against the normal wild type CHO cells.