Effect of membrane potential on pore formation by the antimicrobial peptide magainin 2 in lipid bilayers

Md Mamun Or Rashid1, Md Mizanur Rahman Moghal1, Md Masum Billah1

  • 1Integrated Bioscience Section, Graduate School of Science and Technology, Shizuoka University, Shizuoka 422-8529, Japan.

Insights

Antimicrobial peptides (AMPs) cause membrane damage. This study shows that magainin 2 (Mag) forms pores more readily in lipid membranes with a negative membrane potential, due to increased peptide binding.

Area of Science:

  • Biophysics
  • Membrane Biology
  • Antimicrobial Peptides

Background:

  • The interaction of antimicrobial peptides (AMPs) with lipid bilayers is crucial for their function.
  • The influence of membrane potential on AMP-induced membrane damage is not fully understood.

Purpose of the Study:

  • To investigate the effect of membrane potential on pore formation by magainin 2 (Mag) in giant unilamellar vesicles (GUVs).
  • To determine how membrane potential influences the binding and activity of Mag.

Main Methods:

  • Studied pore formation by Mag in DOPG/DOPC GUVs under varying membrane potentials generated by K+ gradients.
  • Used fluorescent probes (calcein, CF-Mag, AF647) and confocal laser scanning microscopy (CLSM) to quantify permeation, peptide binding, and localization.

Main Results:

  • The rate of Mag-induced pore formation (k_p) increased with more negative membrane potentials.
  • Mag binding to the membrane, indicated by increased CF-Mag concentration, was enhanced at negative membrane potentials.
  • CF-Mag localized to the external leaflet of GUVs before pore formation.

Conclusions:

  • Increased surface concentration of Mag at negative membrane potentials is a primary driver for enhanced pore formation.
  • Membrane potential significantly modulates the interaction of magainin 2 with lipid membranes, affecting its pore-forming activity.

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