Lacticin Q is an antimicrobial peptide that forms pores on membranes. We investigated effects of negatively charged lipids on the binding and pore formation of lacticin Q with liposomes by surface plasmon resonance analysis and fluorescence dye leakage experiments respectively. Negatively charged lipids accelerated the binding of lacticin Q on the membranes and the resulting pore formation. However, the acceleration was not an essential factor in the killing activity of lacticin Q, since pore-forming activities against electrically neutral and negatively charged liposomes occurred similarly.
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