Helical Hairpin Structure of a Potent Antimicrobial Peptide MSI-594 in Lipopolysaccharide Micelles by NMR Spectroscopy

被引：86

作者：

Bhunia, Anirban ^{[2
]}

Ramamoorthy, Ayyalusamy ^{[1
]}

Bhattacharjya, Surajit ^{[2
]}

机构：

[1] Univ Michigan, Dept Chem & Biophys, Ann Arbor, MI 48109 USA

[2] Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore

来源：

CHEMISTRY-A EUROPEAN JOURNAL | 2009年 / 15卷 / 09期

关键词：

antibiotics; lipopolysaccharides; NMR spectroscopy; peptides; SEQUENCE ALTERATION; LIGAND-BINDING; MEMBRANE; MSI-78; CONFORMATIONS; DIASTEREOMERS; MECHANISM; OLIGOMERS; MELITTIN; BILAYERS;

D O I：

10.1002/chem.200802635

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Three dimensional (3D) helical hairpin structure of a highly active antimicrobial peptide MSI-594 in lipopolysaccharide (LPS) micelles using transferred nuclear Overhauser effect (Tr-NOE) or exchanged transferred nuclear Overhauser effect (Et-NOE) spectroscopy was presented. The hybrid MSI-594 was derived based on the premise that the cationic N-terminus of MSI-78 provide binding to negatively charged membrane head groups. Medium range NOEs are observed between amide protons of the carboxylic group of residue 1.24 with T21C/H3. The structure and interactions of MSI-594 peptide with LPS provides novel insights into a potent antomicrobial peptide overcoming the LPS barrier. It is also found that the positively charged groups of Lys residues across the two helices maintain a typical distance range of 12 to 15 Å.

引用

页码：2036 / 2040

页数：5