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Fallaxin analogues with improved antibacterial activity

  • S. L. Nielsen
  • N. Frimodt-Møller
  • P. R. Hansen
Part of the Advances in Experimental Medicine and Biology book series (volume 611)

Introduction

The antibacterial peptide ”fallaxin” H-GVVDILKGAAKDIAGHLASKVMNKL-NH2, recently isolated from the West-Indian mountain chicken frog ”leptodactylus fallax”, have been shown to inhibit the growth of a number of Gram-negative bacteria including E.coli, P.aeruginosa and K.pneumoniae [1]. Antibacterial activity and selectivity has in studies shown to depend on various parameters i.e. the net charge, mean hydrophobicity <H>, mean hydrophobic moment <μH> and the ability to fold into amphipatic structures upon interaction with membrane models [2]. To gain further insight into the structure-activity relationship of fallaxin, we performed a complete alanine-scan of fallaxin. The peptides were tested for antibacterial activity against methicilin-resistant S.aureus (MRSA), vancomycin-intermediate resistant S.aureus, (VISA), E.coli and K.pneumoniae. Finally, the cytotoxicity of the fallaxin analogues against human erythrocytes was assessed in a hemolytic activity assay

Results and...

Keywords

Antibacterial Activity Human Erythrocyte Activity Profile Peptide Synthesis Hemolytic Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

SLN gratefully acknowledges a scholarship from Novozymes/Novo-Nordisk.

References

  1. 1.
    Rollins-Smith, L.A., et al. (2005) An Antimicrobial peptide from the skin secretions of the mountain chicken frog Leptodactulys fallax (Anura: Leptodactylidae) Regulatory Peptides 124: 173–179CrossRefGoogle Scholar
  2. 2.
    Hancock, R.E.W., and Sahl, H.G., (2006). Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nature Biotechnology 24: 1551–1557.CrossRefGoogle Scholar
  3. 3.
    Nielsen, S.L., et al. (2007) Structure-activity study of the antibacterial peptide fallaxin. Protein Science 16: 1969–1976.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • S. L. Nielsen
    • 1
  • N. Frimodt-Møller
    • 2
  • P. R. Hansen
    • 1
  1. 1.Department of Natural Sciences, Faculty of Life SciencesUniversity of CopenhagenDenmark
  2. 2.National Center for Antimicrobials and Infection ControlStatens Serum InstitutDenmark

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