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Antimicrobial peptide dendrimer interacts with phosphocholine membranes in a fluidity dependent manner: a neutron reflection study combined with molecular dynamics simulations.

Lind, Tania LU ; Darré, L; Domene, C; Urbanczyk-Lipkowska, Z; Cárdenas, M and Wacklin, H P (2015) In Biochimica et Biophysica Acta 1848(10). p.2075-2084
Abstract
The interaction mechanism of a novel amphiphilic antimicrobial peptide dendrimer, BALY, with model lipid bilayers was explored through a combination of neutron reflection and molecular dynamics simulations. 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1,2-dipalmitoyl-sn-glycero-3-phos-phocholine (DPPC) lipid bilayers were examined at room temperature to extract information on the interaction of BALY with fluid and gel phases, respectively. Furthermore, a 1:4 mixture of POPC and DPPC was used as a model of a phase-separated membrane. Upon interaction with fluid membranes, BALY inserted in the distal leaflet and caused thinning and disordering of the headgroups. Membrane thinning and expansion of the lipid cross-sectional area... (More)
The interaction mechanism of a novel amphiphilic antimicrobial peptide dendrimer, BALY, with model lipid bilayers was explored through a combination of neutron reflection and molecular dynamics simulations. 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1,2-dipalmitoyl-sn-glycero-3-phos-phocholine (DPPC) lipid bilayers were examined at room temperature to extract information on the interaction of BALY with fluid and gel phases, respectively. Furthermore, a 1:4 mixture of POPC and DPPC was used as a model of a phase-separated membrane. Upon interaction with fluid membranes, BALY inserted in the distal leaflet and caused thinning and disordering of the headgroups. Membrane thinning and expansion of the lipid cross-sectional area was observed for gel phase membranes, also with limited insertion to the distal leaflet. However, dendrimer insertion through the entire lipid tail region was observed upon crossing the lipid phase transition temperature of DPPC and in phase separated membranes. The results show clear differences in the interaction mechanism of the dendrimer depending on the lipid membrane fluidity, and suggest that a role for lipid phase separation in promoting its antimicrobial activity. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochimica et Biophysica Acta
volume
1848
issue
10
pages
2075 - 2084
publisher
Elsevier
external identifiers
  • pmid:26025586
  • wos:000362153400015
  • scopus:84936870727
ISSN
0006-3002
DOI
10.1016/j.bbamem.2015.05.015
language
English
LU publication?
yes
id
3ad83ce6-58df-46c7-a6a0-a2cf58b9a950 (old id 5436240)
date added to LUP
2015-06-12 14:03:16
date last changed
2017-11-05 04:04:51
@article{3ad83ce6-58df-46c7-a6a0-a2cf58b9a950,
  abstract     = {The interaction mechanism of a novel amphiphilic antimicrobial peptide dendrimer, BALY, with model lipid bilayers was explored through a combination of neutron reflection and molecular dynamics simulations. 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1,2-dipalmitoyl-sn-glycero-3-phos-phocholine (DPPC) lipid bilayers were examined at room temperature to extract information on the interaction of BALY with fluid and gel phases, respectively. Furthermore, a 1:4 mixture of POPC and DPPC was used as a model of a phase-separated membrane. Upon interaction with fluid membranes, BALY inserted in the distal leaflet and caused thinning and disordering of the headgroups. Membrane thinning and expansion of the lipid cross-sectional area was observed for gel phase membranes, also with limited insertion to the distal leaflet. However, dendrimer insertion through the entire lipid tail region was observed upon crossing the lipid phase transition temperature of DPPC and in phase separated membranes. The results show clear differences in the interaction mechanism of the dendrimer depending on the lipid membrane fluidity, and suggest that a role for lipid phase separation in promoting its antimicrobial activity.},
  author       = {Lind, Tania and Darré, L and Domene, C and Urbanczyk-Lipkowska, Z and Cárdenas, M and Wacklin, H P},
  issn         = {0006-3002},
  language     = {eng},
  number       = {10},
  pages        = {2075--2084},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta},
  title        = {Antimicrobial peptide dendrimer interacts with phosphocholine membranes in a fluidity dependent manner: a neutron reflection study combined with molecular dynamics simulations.},
  url          = {http://dx.doi.org/10.1016/j.bbamem.2015.05.015},
  volume       = {1848},
  year         = {2015},
}