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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
Institute of Chemistry and Nano-Science Center, University of Copenhagen, Universitetsparken 5, DK 2100 Copenhagen, Denmark; European Spallation Source ESS AB, P.O. Box 176, 22100 Lund, Sweden.
Department of Chemistry, King's College London, London SE1 9NH, UK.
Department of Chemistry, King's College London, London SE1 9NH, UK; Chemistry Research Laboratory, Mansfield Road, University of Oxford, Oxford OX1 3TA, UK.
Institute of Organic Chemistry, Polish Academy of Sciences, 01-224 Warsaw, Poland.
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2015 (English)In: Biochimica et Biophysica Acta - Biomembranes, ISSN 0005-2736, E-ISSN 1879-2642, Vol. 1848, no 10, p. 2075-2084Article in journal (Refereed) Published
Abstract [en]

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 were 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 a role for lipid phase separation in promoting its antimicrobial activity.

Place, publisher, year, edition, pages
Elsevier, 2015. Vol. 1848, no 10, p. 2075-2084
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Natural Sciences
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URN: urn:nbn:se:mau:diva-4128DOI: 10.1016/j.bbamem.2015.05.015ISI: 000362153400015PubMedID: 26025586Scopus ID: 2-s2.0-84936870727Local ID: 19814OAI: oai:DiVA.org:mau-4128DiVA, id: diva2:1400953
Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2025-01-13Bibliographically approved

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Lind, TKCárdenas, Marité

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