Effects of topology, length, and charge on the activity of a kininogen-derived peptide on lipid membranes and bacteria

Lovisa Ringstad, Lukasz Kacprzyk, Artur Schmidtchen, Martin Malmsten

Research output: Contribution to journalArticlepeer-review

Abstract

Effects of topology, length, and charge on peptide interactions with lipid bilayers was investigated for variants of the human kininogen-derived peptide HKH20 (HKHGHGHGKHKNKGKKNGKH) by ellipsometry, CD, fluorescence spectroscopy, and z-potential measurements. The peptides display primarily random coil conformation in buffer and at lipid bilayers, and their lipid interaction is dominated by electrostatics, the latter evidenced by higher peptide adsorption and resulting membrane rupture for an anionic than for a zwitterionic membrane, as well as by strongly reduced adsorption and membrane rupture at high ionic strength. At sufficiently high peptide charge density, however, electrostatic interactions contribute to reducing the peptide adsorption and membrane defect formation. Truncating HKE20 into overlapping 10 amino acid peptides resulted in essentially eliminated membrane rupture and in a reduced amount peptide charges pinned at the lipid bilayer. Finally, cyclic HKH20 was found to be less efficient than the linear peptide in causing liposome rupture, partly due to a lower adsorption. Analogous results were found regarding bactericidal effects.
Original languageEnglish
Pages (from-to)715-727
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1768
Issue number3
DOIs
Publication statusPublished - 2007

Subject classification (UKÄ)

  • Dermatology and Venereal Diseases

Free keywords

  • liposome
  • ellipsometry
  • bacteria
  • adsorption
  • antimicrobial
  • membrane
  • peptide

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