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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles

  • Jung, Hyun-Ho (Department of Life Science, Gwangju Institute of Science and Technology) ;
  • Yang, Sung-Tae (Section on Membrane Biology, Laboratory of Cellular and Molecular Biophysics, National Institute of Child Health and Human Development, National Institutes of Health) ;
  • Sim, Ji-Yeong (Department of Life Science, Gwangju Institute of Science and Technology) ;
  • Lee, Seung-Kyu (Department of Life Science, Gwangju Institute of Science and Technology) ;
  • Lee, Ju-Yeon (Department of Life Science, Gwangju Institute of Science and Technology) ;
  • Kim, Ha-Hyung (College of Pharmacy, Chung-Ang University) ;
  • Shin, Song-Yub (Department of Bio-Materials, Graduate School and Department of Cellular & Molecular Medicine, School of Medicine, Chosun University) ;
  • Kim, Jae-Il (Department of Life Science, Gwangju Institute of Science and Technology)
  • Received : 2010.04.08
  • Accepted : 2010.04.15
  • Published : 2010.05.31
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Abstract

Dermcidin is a human antibiotic peptide that is secreted by the sweat glands and has no homology to other known antimicrobial peptides. As an initial step toward understanding dermcidin's mode of action at bacterial membranes, we used homonuclear and heteronuclear NMR to determine the conformation of the peptide in 50% trifluoroethanol solution. We found that dermcidin adopts a flexible amphipathic $\alpha$-helical structure with a helix-hinge-helix motif, which is a common molecular fold among antimicrobial peptides. Spin-down assays of dermcidin and several related peptides revealed that the affinity with which dermcidin binds to bacterial-mimetic membranes is primarily dependent on its amphipathic $\alpha$-helical structure and its length (>30 residues); its negative net charge and acidic pI have little effect on binding. These findings suggest that the mode of action of dermcidin is similar to that of other membrane-targeting antimicrobial peptides, though the details of its antimicrobial action remain to be determined.

Keywords

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