Action of antimicrobial peptides into the bacterial outer membrane, activity enhancement, and the technology for single molecular evaluation

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The interaction of lipopolysaccharide(LPS) and its hydrophobic part lipid A with antimicrobial peptides or bile acids was studied. We elucidated the conformation of their phosphate groups due to peptide binding, and the profile of the secondary structure of the peptides by physicochemical analyses. The thermodynamics of binding between peptides and lipid A showed that the acidic amino acid substituted peptides improved the binding activity. The conformation change of the peptide enhanced the ability of incorporation into the lipid A aggregates, along with changes in biochemical and biophysical parameters. The surface enhanced Raman scattering spectroscopy study indicated the applicability of that to the LPS evaluation.