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

被引:110
作者
Schibli, DJ [1 ]
Hwang, PM [1 ]
Vogel, HJ [1 ]
机构
[1] Univ Calgary, Dept Biol Sci, Calgary, AB T2N 1N4, Canada
基金
英国医学研究理事会;
关键词
lactoferricin B; antimicrobial peptide; nuclear magnetic resonance structure; micelle; tryptophan;
D O I
10.1016/S0014-5793(99)00214-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 Gin residues, (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:213 / 217
页数:5
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