Effects of topology, length, and charge on the activity of a kininogen-derived peptide on lipid membranes and bacteria
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/669952
- author
- Ringstad, Lovisa ; Kacprzyk, Lukasz ; Schmidtchen, Artur LU and Malmsten, Martin LU
- organization
- publishing date
- 2007
- 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
- 2016-04-01 16:29:44
- date last changed
- 2022-10-13 18:13:02
@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}}, keywords = {{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}}, doi = {{10.1016/j.bbamem.2006.11.016}}, volume = {{1768}}, year = {{2007}}, }