For prokaryotic organisms like bacteria, their interaction with their environment is dominated by the constituent molecules of their outer cell walls or membranes.  The physiochemical properties of these molecules influence how the cells respond to environmental conditions, such as temperature, pH, and salinity (ionic strength), but also how they interact with surfaces.  For Gram negative bacteria, such as Escherichia coli and Yersinia pestis, these molecules are the lipopolysaccharides, found at the outer membrane.  These molecules consist of, for most species and serotypes, a 10-50 heterogeneous chain of polysaccharides anchored to an amphiphilic lipid A core, which embeds it into the inner cell membrane.  Lipid A, with a mostly conserved chemical structure amongst bacterial species, is of particular importance because it the cause of sepsis.  We have investigated the structure/function relationship of LPS and lipid A molecules isolated from Yersinia pestis grown under different environmental conditions towards binding to a small set of immobilized antimicrobial peptides.  Using surface plamson resonance light scattering experiments, we have observed the effects of different LPS and lipid A chemical structures in different environments on both binding to the peptide derived surfaces as well as the aggregation behavior.  Developing a greater fundamental understanding of the interfacial behavior of LPS and lipid A is paramount for applications such as biosensors and bio-resistant surfaces.

Exploring structure/function relationships of bacterial lipopolysaccharides and lipid A with man-made surfaces presenting antimicrobial peptides

248th National Meeting (2014)

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