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Background  There is an urgent need to develop potent antimicrobials for the treatment of infections caused by antibiotic-resistant bacterial pathogens. Paenipeptin C′ (C8-Pat) is a novel linear lipopeptide recently discovered by our group. The objectives of this study were to determine the time-kill kinetics of paenipeptin C′ against  Pseudomonas aeruginosa  ATCC 27853 and  Staphylococcus aureus  ATCC 29213 and to investigate its mechanism of action.    Results  Paenipeptin C′ was synthesized by solid-phase peptide synthesis and purified by HPLC to homogeneity. Paenipeptin C′ showed concentration-dependent bactericidal activity against  P. aeruginosa  and  S. aureus.  Purified lipopolysaccharides (LPS) from the outer membrane of Gram-negative bacteria and lipoteichoic acid (LTA) from Gram-positive bacteria significantly decreased the antibacterial activity of paenipeptin C′, which indicated that LPS and LTA on cell surfaces are likely the initial binding targets of this antibiotic agent. Moreover, paenipeptin C′ damaged bacterial cytoplasmic membranes, as evidenced by the depolarization of membrane potential and leakage of intracellular potassium ions. Specifically, paenipeptin C′ at 32–64 μg/mL caused a significant membrane potential depolarization in  P. aeruginosa  and  S. aureus . This antibiotic at 64–128 μg/mL rapidly induced the release of intracellular potassium ions from  P. aeruginosa  and  S. aureus . Transmission electron microscopy imaging results showed that paenipeptin C′ at bactericidal concentrations perturbed the cell envelopes, leading to the loss of intracellular contents.    Conclusions  Therefore, paenipeptin C' exerts its bactericidal effect through damaging bacterial cytoplasmic membrane.

bmc microbiology

Novel linear lipopeptide paenipeptin C′ binds to lipopolysaccharides and lipoteichoic acid and exerts bactericidal activity by the disruption of cytoplasmic membrane