Interactions between a quadruply-charged X-shaped peptide and bacterial Lipopolysaccharides (LPS) micelles: Complexation or penetration

Lipopolysaccharides (LPS) is the main component (~75%) of the Gram-negative bacteria outer membrane which can trigger lethal septic shocks when released into a host’s bloodstream. Oligoglycine tetramer is a cationic four-armed X-shaped synthetic peptide with quadruple charges. The anionic phosphorylated and carboxylated headgroup can be targeted by the X-peptides, conjectured to reduce bacterial virulence via shielding its viral adhesion receptor, as well as affecting the elastic properties and structural integrity of bacterial membranes. We propose a SANS study of the interactions of LPS micelles mediated by the X-peptides, varying the concentration, solution pH and temperature, as well as the LPS architecture. The unprecedented results will underpin understanding of the efficacy of the X-peptide as an antimicrobial peptide in compromising the bacteria membrane structure.