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A biophysical study...
A biophysical study of the interactions between the antimicrobial peptide indolicidin and lipid model systems
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- Nielsen, Josefine Eilsø (författare)
- Department of Chemistry, University of Oslo, 0315 Oslo, Norway
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- Lind, Tania Kjellerup (författare)
- Malmö universitet,Institutionen för biomedicinsk vetenskap (BMV),Biofilms Research Center for Biointerfaces
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- Lone, Abdullah (författare)
- Department of Science and Environment, Roskilde University, 4000 Roskilde, Denmark
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- Gerelli, Yuri (författare)
- Institut Laue - Langevin, 38000 Grenoble, France
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- Hansen, Paul Robert (författare)
- Department of Drug Design and Pharmacology, University of Copenhagen, 2100 Copenhagen, Denmark
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- Jenssen, Håvard (författare)
- Department of Science and Environment, Roskilde University, 4000 Roskilde, Denmark
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- Cárdenas, Marité (författare)
- Malmö universitet,Institutionen för biomedicinsk vetenskap (BMV),Biofilms Research Center for Biointerfaces
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- Lund, Reidar (författare)
- Department of Chemistry, University of Oslo, 0315 Oslo, Norway
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(creator_code:org_t)
- Elsevier, 2019
- 2019
- Engelska.
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Ingår i: Biochimica et Biophysica Acta - Biomembranes. - : Elsevier. - 0005-2736 .- 1879-2642. ; 1861:7, s. 1355-1364
- Relaterad länk:
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https://doi.org/10.1...
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https://mau.diva-por... (primary) (Raw object)
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https://doi.org/10.1...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
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- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Biochemistry & Molecular Biology
- Biophysics
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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