Designing a short, potent, pore-forming antimicrobial peptide

Antimicrobial peptides (AMPs) are considered as promising candidates to combat emergence of multidrug-resistant bacteria. However, they usually have complex structures and are expensive to produce. Herein we design a short, potent, pore-forming antibacterial peptide utilizing the two basic features of AMPs: cationicity and hydrophobicity. The designed peptide, KLR is evaluated for its antibacterial potency. The results reveal that KLR is a potent AMP that inhibits growth of E. coli and S. aureus with minimal inhibitory concentration (MIC) similar to that of full-length AMPs and is non-toxic towards mammalian cells. We also show that KLR kills bacteria by forming membrane pores making it less susceptible to development of bacterial resistance.