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An electrochemical study into the interaction between complement-derived peptides and DOPC mono- and bilayers.

Lovisa Ringstad1, Elisabeth Protopapa, Britta Lindholm-Sethson

  • 1Department of Pharmacy, Uppsala University, Uppsala, Sweden. lovisa.ringstad@farmaci.uu.se

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Summary

Antimicrobial peptides (CNY21 variants) interact with lipid membranes, with hydrophobicity driving deeper penetration and increased permeability. This suggests local membrane defects, not just pore formation, are key to their action.

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Area of Science:

  • Biophysical Chemistry
  • Membrane Biophysics
  • Antimicrobial Peptides

Background:

  • Antimicrobial peptides are crucial in innate immunity.
  • Understanding peptide-membrane interactions is vital for drug development.
  • Complement-derived peptide CNY21 is a model for studying these interactions.

Purpose of the Study:

  • To investigate the interaction of CNY21 peptide variants with dioleoyl phosphatidylcholine (DOPC) lipid monolayers.
  • To determine how peptide hydrophobicity and charge affect membrane penetration and permeability.
  • To elucidate the mechanism of action of CNY21 peptides on lipid membranes.

Main Methods:

  • Electrochemical techniques (hanging mercury drop electrode, capacitance potential, impedance measurements).
  • Study of electroactive ion permeability (Tl+, Pb2+, Cd2+, Eu3+).
  • Liposome leakage assays, circular dichroism, and ellipsometry for bilayer studies.

Main Results:

  • CNY21 variants interact with DOPC monolayers, with hydrophobic variants penetrating deeper.
  • Increased hydrophobicity enhanced monolayer permeability to ions.
  • Charge influenced peptide localization, with higher positive charge limiting penetration to the headgroup region.
  • Peptide-induced membrane defects, rather than solely pore formation, are critical for peptide activity.

Conclusions:

  • Peptide hydrophobicity is a key determinant of membrane interaction and permeabilization.
  • Charge repulsion, not ion size, governs cation passage through peptide-induced defects.
  • The mechanism involves local membrane packing defects, not just transmembrane pore formation.