Defects in the Core Oligosaccharide in Gram Negative Bacterial Outer Membrane Models Expose Anionic Binding Sites, A Potential Achilles Heel

DOI

The outer membrane of Gram negative bacterial is an effective barrier for many harmful agents. We have been developing and testing advanced models of the Gram negative bacterial outer surface to understand the biochemistry of this important biological surface with molecular precision. So how do cationic antimicrobial agents bind to the anionic phosphate groups of the Lipopolysaccharides (LPS) during their membrane disruption activity? Here, using neutron reflectometry we intend to induce holes in the core region of a model asymmetric gram negative bacterial outer membrane and, using a new titration technique we have developed, examine the Debye screening lengths of the electrostatic bonds formed between a cationic antimicrobial protein (colicin N) and the anionic phosphate groups of the core oligosaccharides of LPS. We hypothesise that the holes allow for short range electrostatic bonds.

Identifier
DOI https://doi.org/10.5286/ISIS.E.100725433
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/100725433
Provenance
Creator Dr Luke Clifton; Dr Nico Paracini; Dr Maxmilian Skoda; Professor Jeremy Lakey
Publisher ISIS Neutron and Muon Source
Publication Year 2021
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 2018-12-10T08:00:00Z
Temporal Coverage End 2018-12-14T08:39:55Z