A biophysical study of the interactions between the antimicrobial peptide indolicidin and lipid model systems

Josefine Eilsø Nielsen, Tania Kjellerup Lind, Abdullah Lone, Yuri Gerelli, Paul Robert Hansen, Håvard Jenssen, Marité Cárdenas, Reidar Lund

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

The naturally occurring peptide indolicidin from bovine neutrophils exhibits strong biological activity against a broad spectrum of microorganisms. This is believed to arise from selective interactions with the negatively charged cytoplasmic lipid membrane found in bacteria. We have investigated the peptide interaction with supported lipid model membranes using a combination of complementary surface sensitive techniques: neutron reflectometry (NR), atomic force microscopy (AFM), and quartz crystal microbalance with dissipation monitoring (QCM-D). The data are compared with small-angle X-ray scattering (SAXS) results obtained with lipid vesicle/peptide solutions. The peptide membrane interaction is shown to be significantly concentration dependent. At low concentrations, the peptide inserts at the outer leaflet in the interface between the headgroup and tail core. Insertion of the peptide results in a slight decrease in the lipid packing order of the bilayer, although not sufficient to cause membrane thinning. By increasing the indolicidin concentration well above the physiologically relevant conditions, a deeper penetration of the peptide into the bilayer and subsequent lipid removal take place, resulting in a slight membrane thinning. The results suggest that indolicidin induces lipid removal and that mixed indolicidin-lipid patches form on top of the supported lipid bilayers. Based on the work presented using model membranes, indolicidin seems to act through the interfacial activity model rather than through the formation of stable pores.
OriginalsprogEngelsk
TidsskriftB B A - Biomembranes
Vol/bind1861
Udgave nummer7
Sider (fra-til)1355-1364
Antal sider10
ISSN0005-2736
DOI
StatusUdgivet - 2019

Citer dette

Nielsen, Josefine Eilsø ; Lind, Tania Kjellerup ; Lone, Abdullah ; Gerelli, Yuri ; Hansen, Paul Robert ; Jenssen, Håvard ; Cárdenas, Marité ; Lund, Reidar. / A biophysical study of the interactions between the antimicrobial peptide indolicidin and lipid model systems. I: B B A - Biomembranes. 2019 ; Bind 1861, Nr. 7. s. 1355-1364.
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title = "A biophysical study of the interactions between the antimicrobial peptide indolicidin and lipid model systems",
abstract = "The naturally occurring peptide indolicidin from bovine neutrophils exhibits strong biological activity against a broad spectrum of microorganisms. This is believed to arise from selective interactions with the negatively charged cytoplasmic lipid membrane found in bacteria. We have investigated the peptide interaction with supported lipid model membranes using a combination of complementary surface sensitive techniques: neutron reflectometry (NR), atomic force microscopy (AFM), and quartz crystal microbalance with dissipation monitoring (QCM-D). The data are compared with small-angle X-ray scattering (SAXS) results obtained with lipid vesicle/peptide solutions. The peptide membrane interaction is shown to be significantly concentration dependent. At low concentrations, the peptide inserts at the outer leaflet in the interface between the headgroup and tail core. Insertion of the peptide results in a slight decrease in the lipid packing order of the bilayer, although not sufficient to cause membrane thinning. By increasing the indolicidin concentration well above the physiologically relevant conditions, a deeper penetration of the peptide into the bilayer and subsequent lipid removal take place, resulting in a slight membrane thinning. The results suggest that indolicidin induces lipid removal and that mixed indolicidin-lipid patches form on top of the supported lipid bilayers. Based on the work presented using model membranes, indolicidin seems to act through the interfacial activity model rather than through the formation of stable pores.",
author = "Nielsen, {Josefine Eils{\o}} and Lind, {Tania Kjellerup} and Abdullah Lone and Yuri Gerelli and Hansen, {Paul Robert} and H{\aa}vard Jenssen and Marit{\'e} C{\'a}rdenas and Reidar Lund",
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A biophysical study of the interactions between the antimicrobial peptide indolicidin and lipid model systems. / Nielsen, Josefine Eilsø; Lind, Tania Kjellerup; Lone, Abdullah; Gerelli, Yuri; Hansen, Paul Robert; Jenssen, Håvard; Cárdenas, Marité; Lund, Reidar.

I: B B A - Biomembranes, Bind 1861, Nr. 7, 2019, s. 1355-1364.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - A biophysical study of the interactions between the antimicrobial peptide indolicidin and lipid model systems

AU - Nielsen, Josefine Eilsø

AU - Lind, Tania Kjellerup

AU - Lone, Abdullah

AU - Gerelli, Yuri

AU - Hansen, Paul Robert

AU - Jenssen, Håvard

AU - Cárdenas, Marité

AU - Lund, Reidar

PY - 2019

Y1 - 2019

N2 - The naturally occurring peptide indolicidin from bovine neutrophils exhibits strong biological activity against a broad spectrum of microorganisms. This is believed to arise from selective interactions with the negatively charged cytoplasmic lipid membrane found in bacteria. We have investigated the peptide interaction with supported lipid model membranes using a combination of complementary surface sensitive techniques: neutron reflectometry (NR), atomic force microscopy (AFM), and quartz crystal microbalance with dissipation monitoring (QCM-D). The data are compared with small-angle X-ray scattering (SAXS) results obtained with lipid vesicle/peptide solutions. The peptide membrane interaction is shown to be significantly concentration dependent. At low concentrations, the peptide inserts at the outer leaflet in the interface between the headgroup and tail core. Insertion of the peptide results in a slight decrease in the lipid packing order of the bilayer, although not sufficient to cause membrane thinning. By increasing the indolicidin concentration well above the physiologically relevant conditions, a deeper penetration of the peptide into the bilayer and subsequent lipid removal take place, resulting in a slight membrane thinning. The results suggest that indolicidin induces lipid removal and that mixed indolicidin-lipid patches form on top of the supported lipid bilayers. Based on the work presented using model membranes, indolicidin seems to act through the interfacial activity model rather than through the formation of stable pores.

AB - The naturally occurring peptide indolicidin from bovine neutrophils exhibits strong biological activity against a broad spectrum of microorganisms. This is believed to arise from selective interactions with the negatively charged cytoplasmic lipid membrane found in bacteria. We have investigated the peptide interaction with supported lipid model membranes using a combination of complementary surface sensitive techniques: neutron reflectometry (NR), atomic force microscopy (AFM), and quartz crystal microbalance with dissipation monitoring (QCM-D). The data are compared with small-angle X-ray scattering (SAXS) results obtained with lipid vesicle/peptide solutions. The peptide membrane interaction is shown to be significantly concentration dependent. At low concentrations, the peptide inserts at the outer leaflet in the interface between the headgroup and tail core. Insertion of the peptide results in a slight decrease in the lipid packing order of the bilayer, although not sufficient to cause membrane thinning. By increasing the indolicidin concentration well above the physiologically relevant conditions, a deeper penetration of the peptide into the bilayer and subsequent lipid removal take place, resulting in a slight membrane thinning. The results suggest that indolicidin induces lipid removal and that mixed indolicidin-lipid patches form on top of the supported lipid bilayers. Based on the work presented using model membranes, indolicidin seems to act through the interfacial activity model rather than through the formation of stable pores.

U2 - 10.1016/j.bbamem.2019.04.003

DO - 10.1016/j.bbamem.2019.04.003

M3 - Journal article

VL - 1861

SP - 1355

EP - 1364

JO - B B A - Biomembranes

JF - B B A - Biomembranes

SN - 0005-2736

IS - 7

ER -