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

研究了脂多糖（LPS）及其疏水部分类脂A与抗菌肽或胆汁酸的相互作用。我们阐明了它们的磷酸基团的构象，由于肽结合，并通过理化分析的肽的二级结构的配置文件。肽与脂质A结合的热力学研究表明，酸性氨基酸取代的肽提高了结合活性。肽的构象变化增强了掺入脂质A聚集体的能力，沿着生物化学和生物物理参数的变化。表面增强拉曼散射光谱研究表明，LPS的评价的适用性。

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.