Schibli D J, Hwang P M, Vogel H J
Department of Biological Sciences, University of Calgary, Canada.
FEBS Lett. 1999 Mar 12;446(2-3):213-7. doi: 10.1016/s0014-5793(99)00214-8.
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.
乳铁蛋白B（LfcinB）是一种由胃蛋白酶消化牛乳铁蛋白后释放出的含25个氨基酸残基的抗菌肽。LfcinB的抗菌中心由六个氨基酸残基（RRWQWR-NH2）组成，并且它具有与LfcinB相似的杀菌活性。通过核磁共振光谱和分子动力学精修确定了与十二烷基硫酸钠（SDS）胶束结合的六肽结构。当该肽与SDS胶束结合时，它呈现出明确的两亲结构，色氨酸侧链与精氨酸残基分离。其他证据表明，该肽在胶束中的取向使得色氨酸残基比精氨酸和谷氨酰胺残基更深地埋在胶束中。
