Abstract
The anticancer activity of anti-bacterial cecropins makes them potentially useful as peptide anti-cancer drugs. We used the cell-attached patch to study the effect of cecropin B (CB; having one hydrophobic and one amphipathic α-helix) and its derivative, cecropin B 3 (CB 3; having two hydrophobic a-helices) on the membrane of Ags cancer cells. Application of 10-60 μM CB onto the membrane of the cancer cell produces short outward currents. Comparative study with CB 3, which induces no outward currents, shows that the amphipathic group of CB is necessary for the pore formation. The results provide a rationale to study the cell-killing activity of antimi-crobial peptides at the single cancer cell level.
