期刊
BIOPHYSICAL CHEMISTRY
卷 150, 期 1-3, 页码 80-87出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2010.01.009
关键词
Aggregate structure; Antimicrobial peptide; Calorimetry; Endotoxin; Lipopolysaccharide; Small-angle X-ray scattering
资金
- Deutsche Forschungsgemeinschaft DFG [SFB617]
- German ministry for Education
- Research BMBF [01GU0824]
- Japan Society for the Promotion of Science (JSPS)
- Grants-in-Aid for Scientific Research [21550168] Funding Source: KAKEN
An analysis of the interaction of the NK-lysin derived peptide NK-2 and of analogs thereof with bacterial lipopolysaccharide (LPS, endotoxin) was performed to determine the most important biophysical parameters for an effective LPS neutralization. We used microcalorimetry, FTIR spectroscopy, Zeta potential measurements, and small-angle X-ray scattering to analyze the peptide:LPS binding enthalpy, the accessible LPS surface charge, the fluidity of the LPS hydrocarbon chains, their phase transition enthalpy change, the aggregate structure of LPS, and how these parameters are modulated by the peptides. We conclude that (i) a high peptide:LPS binding affinity, which is facilitated by electrostatic and hydrophobic interactions and which leads to a positive Zeta potential, (ii) the formation of peptide-enriched domains, which destabilize the lipid packing, demonstrated by a drastic decrease of phase transition enthalpy change of LPS, and (iii) the multilamellarization of the LPS aggregate structure are crucial for an effective endotoxin neutralization by cationic peptides. (C) 2010 Elsevier B.V. All rights reserved.
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