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

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.

Antimicrobial peptides from C-terminal amphipathic region of E. coli FtsA.

Antimicrobial peptides constitute an indispensable component of innate immune system in organisms ranging from bacteria to man. Despite this, peptides lag far behind the conventional antibiotics in treating infections. The menace of multidrug-resistant bacteria, however, has revived the antimicrobial peptide research.

Interaction of MreB-derived antimicrobial peptides with membranes.

Antimicrobial peptides are critical components of defense systems in living forms. The activity is conferred largely by the selective membrane-permeabilizing ability. In our earlier work, we derived potent antimicrobial peptides from the 9-residue long, N-terminal amphipathic helix of E.

Highly potent antimicrobial peptides from N-terminal membrane-binding region of E. coli MreB.

Microbial pathogenesis is a serious health concern. The threat escalates as the existing conventional antimicrobials are losing their efficacy against the evolving pathogens. Peptides hold promise to be developed into next-generation antibiotics.