Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method

Anal Sci. 2016;32(1):57-60. doi: 10.2116/analsci.32.57.


This study describes the pore-forming properties of magainin 1 in planar lipid bilayers. These bilayers were prepared by the droplet contact method, which was executed on a microfabricated device for a high-throughput study. We arrayed four droplet chambers parallelly in the single device, and the current measurements were carried out simultaneously. Using this system, we measured the channel current conductance of magainin 1. We determined the pore size and the number of assembling monomers in magainin pores in mammalian and bacterial model membranes. This system is a powerful tool for analyzing transmembrane peptides and their antimicrobial activities.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antimicrobial Cationic Peptides / analysis*
  • Electric Conductivity
  • Lab-On-A-Chip Devices*
  • Lipid Bilayers / chemistry*
  • Magainins / analysis
  • Membranes, Artificial*
  • Microfluidic Analytical Techniques / methods*
  • Models, Theoretical
  • Molecular Sequence Data
  • Patch-Clamp Techniques
  • Permeability
  • Phosphatidylcholines / chemistry
  • Phosphatidylethanolamines / chemistry
  • Phosphatidylglycerols / chemistry
  • Porosity
  • Xenopus Proteins / analysis*
  • Xenopus laevis


  • Antimicrobial Cationic Peptides
  • Lipid Bilayers
  • Magainins
  • Membranes, Artificial
  • Phosphatidylcholines
  • Phosphatidylethanolamines
  • Phosphatidylglycerols
  • Xenopus Proteins
  • magainin 2 peptide, Xenopus
  • magainin 1 peptide, Xenopus
  • 1,2-dioleoyl-sn-glycero-3-phosphoglycerol
  • 1,2-dielaidoylphosphatidylethanolamine
  • 1,2-oleoylphosphatidylcholine