Self-assembling antimicrobial peptides: interactions with model lipid membranes

DOI

We propose to investigate antimicrobial peptides that self-assemble into well-defined nanostructures. Previous SAXS results have shown that the peptides form rather robust platelets/fibers (“nanosheets”) with well-defined dimension of about 100x6x3 nm3 which persist with the attachment of poly(ethylene glycol) (“PEGylation”). Recent investigations have shown that the peptides that form nanosheets exhibit low cytotoxicity but significant antimicrobial action, while unstructured peptides were significantly more toxic and also prone to enzymatic degradation. In order to understand the biological behaviour, the basic physico-chemical characterizations are needed, in particular at surfaces that might provide insight to their cell interactions.

Identifier
DOI https://doi.org/10.5286/ISIS.E.101138375
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/101138375
Provenance
Creator Mr Nico Koenig; Miss Josefine Eilsø Nielsen; Dr Maxmilian Skoda; Professor Marité Cárdenas Gómez; Professor Reidar Lund
Publisher ISIS Neutron and Muon Source
Publication Year 2022
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2019-03-04T09:00:00Z
Temporal Coverage End 2019-03-08T09:18:27Z