The structure of the antimicrobial active center of lactoferricin B bound to sodium dodecyl sulfate micelles

FEBS Letters

Hwang, Peter M.¹  Schibli, David J.¹  Vogel, Hans J.¹ 

[1] Department of Biological Sciences, University of Calgary, Calgary, Alta T2N 1N4, Canada

关键词: Lactoferricin B;    Antimicrobial peptide;    Nuclear magnetic resonance structure;    Micelle;    Tryptophan;    LfcinB;    lactoferricin B;    LfcinB4–9;    residues 4–9 of lactoferricin B;    SDS;    sodium dodecyl sulfate;    DPC;    dodecylphosphocholine;    MIC;    minimum inhibitory concentration;    CD;    circular dichroism;    DSS;    sodium 3-(trimethylsilyl)-1-propanesulfonate;    RP-HPLC;    reverse phase high performance liquid chromatography;    NOE;    nuclear Overhauser enhancement;    NOESY;    nuclear Overhauser enhancement spectroscopy;    TOCSY;    total correlation spectroscopy;   

DOI  :  10.1016/S0014-5793(99)00214-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Lactoferricin B (LfcinB) is a 25-residue antimicrobial peptide released from bovine lactoferrin upon pepsin digestion. The antimicrobial center of LfcinB consists of six residues (RRWQWR-NH₂), and it possesses similar bactericidal activity to LfcinB. The structure of the six-residue peptide bound to sodium dodecyl sulfate (SDS) micelles has been determined by NMR spectroscopy and molecular dynamics refinement. The peptide adopts a well defined amphipathic structure when bound to SDS micelles with the Trp sidechains separated from the Arg residues. Additional evidence demonstrates that the peptide is oriented in the micelle such that the Trp residues are more deeply buried in the micelle than the Arg and Gln residues.

【 授权许可】

Unknown