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Lipid membrane interactions of self-assembling antimicrobial nanofibers: effect of PEGylation
Department of Chemistry, University of Oslo 0315 Oslo Norway.
Department of Chemistry, University of Oslo 0315 Oslo Norway; Jülich Centre for Neutron Science (JCNS) and Institute for Complex Systems (ICS), Forschungszentrum Jülich GmbH 52425 Jülich Germany.
Department of Chemistry & Biochemistry, The University of Texas at Arlington Arlington Texas 76019 USA.
ISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council, Rutherford Appleton Laboratory Harwell Science and Innovation Campus, Didco Oxfordshire OX11 OQX UK.
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2020 (English)In: RSC Advances, E-ISSN 2046-2069, Vol. 10, p. 35329-35340, article id 35329Article in journal (Refereed) Published
Abstract [en]

Supramolecular assembly and PEGylation (attachment of a polyethylene glycol polymer chain) of peptides can be an effective strategy to develop antimicrobial peptides with increased stability, antimicrobial efficacy and hemocompatibility. However, how the self-assembly properties and PEGylation affect their lipid membrane interaction is still an unanswered question. In this work, we use state-of-the-art small angle X-ray and neutron scattering (SAXS/SANS) together with neutron reflectometry (NR) to study the membrane interaction of a series of multidomain peptides, with and without PEGylation, known to self-assemble into nanofibers. Our approach allows us to study both how the structure of the peptide and the membrane are affected by the peptide–lipid interactions. When comparing self-assembled peptides with monomeric peptides that are not able to undergo assembly due to shorter chain length, we found that the nanofibers interact more strongly with the membrane. They were found to insert into the core of the membrane as well as to absorb as intact fibres on the surface. Based on the presented results, PEGylation of the multidomain peptides leads to a slight net decrease in the membrane interaction, while the distribution of the peptide at the interface is similar to the non-PEGylated peptides. Based on the structural information, we showed that nanofibers were partially disrupted upon interaction with phospholipid membranes. This is in contrast with the considerable physical stability of the peptide in solution, which is desirable for an extended in vivo circulation time.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2020. Vol. 10, p. 35329-35340, article id 35329
Keywords [en]
lipid, antimicrobial peptide, neutron reflection
National Category
Biochemistry and Molecular Biology
Research subject
Health and society
Identifiers
URN: urn:nbn:se:mau:diva-18672DOI: 10.1039/D0RA07679AISI: 000573815400038PubMedID: 35515685Scopus ID: 2-s2.0-85092571925OAI: oai:DiVA.org:mau-18672DiVA, id: diva2:1476787
Available from: 2020-10-15 Created: 2020-10-15 Last updated: 2024-06-17Bibliographically approved

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Cárdenas, Marité

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