Effects of single amino acid substitutions on peptide interaction with lipid membranes and bacteria-variants of GKE21, an internal sequence from human LL-37
(2010) In Colloids and Surfaces A: Physicochemical and Engineering Aspects 354(1-3). p.65-71- Abstract
- Effects of helix destabilization on lipid membrane interaction, liposome rupture, and bacterial killing was investigated for variants of the antimicrobial peptide GKE21 (GKEFKRIVQRIKDFLRNLVPR), an internal sequence of human cathelicidin LL-37, by ellipsometry, circular dichroism, fluorescence spectroscopy, and bacterial radial diffusion assay. GKE21 displayed moderate helix induction in buffer, which increased on interaction with phospholipid membranes. Substituting either of the two valines (V) in GKE21 with either proline (P) or D-valine (dV) resulted in helix destabilization, while peptide isoelectric point, net charge at pH 7.4, and mean hydrophobicity remained unchanged. The decreased tendency for helix formation in GKE21 (V -> P,... (More)
- Effects of helix destabilization on lipid membrane interaction, liposome rupture, and bacterial killing was investigated for variants of the antimicrobial peptide GKE21 (GKEFKRIVQRIKDFLRNLVPR), an internal sequence of human cathelicidin LL-37, by ellipsometry, circular dichroism, fluorescence spectroscopy, and bacterial radial diffusion assay. GKE21 displayed moderate helix induction in buffer, which increased on interaction with phospholipid membranes. Substituting either of the two valines (V) in GKE21 with either proline (P) or D-valine (dV) resulted in helix destabilization, while peptide isoelectric point, net charge at pH 7.4, and mean hydrophobicity remained unchanged. The decreased tendency for helix formation in GKE21 (V -> P, V -> dV) resulted in a lower induced (helix-related) amphiphilicity, and correlated to a lower peptide adsorption at supported phospholipid membranes, as well as to decreased peptide-induced liposome leakage, particularly at high electrolyte concentration where conformation-invariant electrostatic interactions are screened. In addition, bacterial killing was reduced for the substituted peptides, indicating that even minor changes in induced peptide amphiphilicity may be of relevance for the bactericidal properties of this type of antimicrobial peptides. (C) 2009 Elsevier B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1589106
- author
- Ringstad, Lovisa ; Schmidtchen, Artur LU and Malmsten, Martin LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- LL-37, Liposome, Ellipsometry, AMP, Antimicrobial peptide
- in
- Colloids and Surfaces A: Physicochemical and Engineering Aspects
- volume
- 354
- issue
- 1-3
- pages
- 65 - 71
- publisher
- Elsevier
- external identifiers
-
- wos:000275351300012
- scopus:73049084108
- ISSN
- 0927-7757
- DOI
- 10.1016/j.colsurfa.2009.04.018
- language
- English
- LU publication?
- yes
- id
- 12ab8e72-818b-40c4-a3d3-d7d531b5d1bd (old id 1589106)
- date added to LUP
- 2016-04-01 14:24:13
- date last changed
- 2022-01-28 00:24:19
@article{12ab8e72-818b-40c4-a3d3-d7d531b5d1bd, abstract = {{Effects of helix destabilization on lipid membrane interaction, liposome rupture, and bacterial killing was investigated for variants of the antimicrobial peptide GKE21 (GKEFKRIVQRIKDFLRNLVPR), an internal sequence of human cathelicidin LL-37, by ellipsometry, circular dichroism, fluorescence spectroscopy, and bacterial radial diffusion assay. GKE21 displayed moderate helix induction in buffer, which increased on interaction with phospholipid membranes. Substituting either of the two valines (V) in GKE21 with either proline (P) or D-valine (dV) resulted in helix destabilization, while peptide isoelectric point, net charge at pH 7.4, and mean hydrophobicity remained unchanged. The decreased tendency for helix formation in GKE21 (V -> P, V -> dV) resulted in a lower induced (helix-related) amphiphilicity, and correlated to a lower peptide adsorption at supported phospholipid membranes, as well as to decreased peptide-induced liposome leakage, particularly at high electrolyte concentration where conformation-invariant electrostatic interactions are screened. In addition, bacterial killing was reduced for the substituted peptides, indicating that even minor changes in induced peptide amphiphilicity may be of relevance for the bactericidal properties of this type of antimicrobial peptides. (C) 2009 Elsevier B.V. All rights reserved.}}, author = {{Ringstad, Lovisa and Schmidtchen, Artur and Malmsten, Martin}}, issn = {{0927-7757}}, keywords = {{LL-37; Liposome; Ellipsometry; AMP; Antimicrobial peptide}}, language = {{eng}}, number = {{1-3}}, pages = {{65--71}}, publisher = {{Elsevier}}, series = {{Colloids and Surfaces A: Physicochemical and Engineering Aspects}}, title = {{Effects of single amino acid substitutions on peptide interaction with lipid membranes and bacteria-variants of GKE21, an internal sequence from human LL-37}}, url = {{http://dx.doi.org/10.1016/j.colsurfa.2009.04.018}}, doi = {{10.1016/j.colsurfa.2009.04.018}}, volume = {{354}}, year = {{2010}}, }