Aromatic-rich C-terminal region of LCI is a potent antimicrobial peptide in itself

Abstract LCI is a 47-residue antimicrobial peptide produced by Bacillus subtilis. The peptide displays potent activity against plant pathogens, Xanthomonas and Pseudomonas. The peptide takes a compact 3-dimensional structure characterized by a four-stranded β-sheet. The peptide is unusually rich in aromatic residues; 10 of the 47 residues are aromatic and 8 of them lie in the C-terminal region, LCI22-47. Here we report the antimicrobial activity of this C-terminal region against Gram-positive and Gram-negative bacteria. The C-terminal-amidated peptide displays potent activity against E. coli, methicillin and gentamicin-resistant S. aureus, and Xanthomonas oryzae pv. oryzae with lethal concentrations ≤4 μM. Membrane-binding assays indicate preferential binding to the negatively-charged lipids. The peptide permeabilizes the outer-membrane of E. coli indicating membrane-permeabilization as one of the mechanisms of killing. Interestingly, however, no inner-membrane permeabilization was observed, indicating that the membrane-permeabilization may not be the sole mechanism of action.