Cell-selective lysis by novel analogues of melittin against human red blood cells and Escherichia coli

Novel analogues of melittin were designed by substituting the leucine residue(s) at the 'd' and 'a' positions of its previously identified leucine zipper motif to understand the lytic activities of melittin antimicrobial peptide against bacteria and mammalian cells. The data revealed that the substitution of hydrophobic leucine residue(s) by lesser hydrophobic alanine residue(s) in the leucine zipper sequence of melittin disturbed its pore-forming activity and mechanism only in hRBCs but not in the tested bacteria.