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

Ringstad, Lovisa; Kacprzyk, Lukasz; Schmidtchen, Artur LU and Malmsten, Martin (2007) In Biochimica et Biophysica Acta - Biomembranes 1768(3). p.715-727
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... (More)
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. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
keywords
liposome, ellipsometry, bacteria, adsorption, antimicrobial, membrane, peptide
in
Biochimica et Biophysica Acta - Biomembranes
volume
1768
issue
3
pages
715 - 727
publisher
Elsevier
external identifiers
  • wos:000245060200036
  • scopus:33847051295
ISSN
0005-2736
DOI
10.1016/j.bbamem.2006.11.016
language
English
LU publication?
yes
id
c15a0407-6963-49ed-b37f-b7e9e0158572 (old id 669952)
date added to LUP
2007-12-18 11:24:33
date last changed
2017-09-10 04:34:22
@article{c15a0407-6963-49ed-b37f-b7e9e0158572,
  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.},
  author       = {Ringstad, Lovisa and Kacprzyk, Lukasz and Schmidtchen, Artur and Malmsten, Martin},
  issn         = {0005-2736},
  keyword      = {liposome,ellipsometry,bacteria,adsorption,antimicrobial,membrane,peptide},
  language     = {eng},
  number       = {3},
  pages        = {715--727},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta - Biomembranes},
  title        = {Effects of topology, length, and charge on the activity of a kininogen-derived peptide on lipid membranes and bacteria},
  url          = {http://dx.doi.org/10.1016/j.bbamem.2006.11.016},
  volume       = {1768},
  year         = {2007},
}