Neutron Reflectivity Study of Antimicrobial Peptides Interacting with Lipopolysaccharide Bacterial Model Membranes

DOI

The outer membrane (OM) of gram negative bacteria is mainly constituted of highly polydisperse and amphiphilic lipopolysaccharide (LPS), an endotoxin which is accompanied by lipids and proteins. LPS is a potent inflammatory activator that can, once released from the bacterium, lead to septic shock in humans. It also plays a crucial role in the stability of the OM, acting as a permeability barrier towards external molecules and drugs. Some cationic human antimicrobial peptides (hAMPs) possess the ability of disrupting LPS and other membrane structures. In our study we want to assess how three structurally diverse hAMPs interact with outer membrane models composed of different chemotypes of LPS. We will use neutron reflectivity techniques in order elucidate the mechanism of action of these human peptides in relation to their diverse 3D structure and the employed LPS chemotype models.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24091101
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24091101
Provenance
Creator Dr Gianluca Bello; Dr Luke Clifton; Mr Richard Harvey; Dr Richard Harvey
Publisher ISIS Neutron and Muon Source
Publication Year 2016
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 Photon- and Neutron Geosciences
Temporal Coverage Begin 2013-07-24T23:00:00Z
Temporal Coverage End 2013-07-29T10:50:07Z