Composition effect on peptide interaction with lipids and bacteria: Variants of C3a peptide CNY21
(2007) In Biophysical Journal 92(1). p.87-98- Abstract
- The effect of peptide hydrophobicity and charge on peptide interaction with model lipid bilayers was investigated for the C3a-derived peptide CNY21 by fluorescence spectroscopy, circular dichroism, ellipsometry, z-potential, and photon correlation spectroscopy measurements. For both zwitterionic and anionic liposomes, the membrane-disruptive potency for CNY21 variants increased with increasing net positive charge and mean hydrophobicity and was completely lost on elimination of all peptide positive charges. Analogous effects of elimination of the peptide positive net charge in particular were found regarding bacteria killing for both Pseudomonas aeruginosa and Bacillus subtilis. The peptides, characterized by moderate helix content both in... (More)
- The effect of peptide hydrophobicity and charge on peptide interaction with model lipid bilayers was investigated for the C3a-derived peptide CNY21 by fluorescence spectroscopy, circular dichroism, ellipsometry, z-potential, and photon correlation spectroscopy measurements. For both zwitterionic and anionic liposomes, the membrane-disruptive potency for CNY21 variants increased with increasing net positive charge and mean hydrophobicity and was completely lost on elimination of all peptide positive charges. Analogous effects of elimination of the peptide positive net charge in particular were found regarding bacteria killing for both Pseudomonas aeruginosa and Bacillus subtilis. The peptides, characterized by moderate helix content both in buffer and when attached to the liposomes, displayed high adsorption for the net positively charged peptide variants, whereas adsorption was nonmeasurable for the uncharged peptide. That electrostatically driven adsorption represents the main driving force for membrane disruption in lipid systems was also demonstrated by a drastic reduction in both liposome leakage and peptide adsorption with increasing ionic strength, and this salt inactivation can be partly avoided by increasing the peptide hydrophobicity. This increased electrolyte resistance translates also to a higher antibacterial effect for the hydrophobically modified variant at high salt concentration. Overall, our findings demonstrate the importance of the peptide adsorption and resulting peptide interfacial density for membrane-disruptive effects of these peptides. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/682362
- author
- Ringstad, Lovisa ; Nordahl, Emma LU ; Schmidtchen, Artur LU and Malmsten, Martin LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biophysical Journal
- volume
- 92
- issue
- 1
- pages
- 87 - 98
- publisher
- Cell Press
- external identifiers
-
- wos:000242754300015
- scopus:33845972609
- ISSN
- 1542-0086
- DOI
- 10.1529/biophysj.106.088161
- language
- English
- LU publication?
- yes
- id
- cf27c5f9-c081-48c4-876b-aee4afddec03 (old id 682362)
- date added to LUP
- 2016-04-01 11:50:37
- date last changed
- 2022-01-26 19:03:33
@article{cf27c5f9-c081-48c4-876b-aee4afddec03,
abstract = {{The effect of peptide hydrophobicity and charge on peptide interaction with model lipid bilayers was investigated for the C3a-derived peptide CNY21 by fluorescence spectroscopy, circular dichroism, ellipsometry, z-potential, and photon correlation spectroscopy measurements. For both zwitterionic and anionic liposomes, the membrane-disruptive potency for CNY21 variants increased with increasing net positive charge and mean hydrophobicity and was completely lost on elimination of all peptide positive charges. Analogous effects of elimination of the peptide positive net charge in particular were found regarding bacteria killing for both Pseudomonas aeruginosa and Bacillus subtilis. The peptides, characterized by moderate helix content both in buffer and when attached to the liposomes, displayed high adsorption for the net positively charged peptide variants, whereas adsorption was nonmeasurable for the uncharged peptide. That electrostatically driven adsorption represents the main driving force for membrane disruption in lipid systems was also demonstrated by a drastic reduction in both liposome leakage and peptide adsorption with increasing ionic strength, and this salt inactivation can be partly avoided by increasing the peptide hydrophobicity. This increased electrolyte resistance translates also to a higher antibacterial effect for the hydrophobically modified variant at high salt concentration. Overall, our findings demonstrate the importance of the peptide adsorption and resulting peptide interfacial density for membrane-disruptive effects of these peptides.}},
author = {{Ringstad, Lovisa and Nordahl, Emma and Schmidtchen, Artur and Malmsten, Martin}},
issn = {{1542-0086}},
language = {{eng}},
number = {{1}},
pages = {{87--98}},
publisher = {{Cell Press}},
series = {{Biophysical Journal}},
title = {{Composition effect on peptide interaction with lipids and bacteria: Variants of C3a peptide CNY21}},
url = {{http://dx.doi.org/10.1529/biophysj.106.088161}},
doi = {{10.1529/biophysj.106.088161}},
volume = {{92}},
year = {{2007}},
}