Structure and mode of action of the antimicrobial peptide arenicin.

@article{Andr2008StructureAM,
  title={Structure and mode of action of the antimicrobial peptide arenicin.},
  author={J{\"o}rg Andr{\"a} and Igor Jakovkin and Joachim Gr{\"o}tzinger and Oliver Hecht and Anna D Krasnosdembskaya and Torsten Goldmann and Thomas Gutsmann and Matthias Leippe},
  journal={The Biochemical journal},
  year={2008},
  volume={410 1},
  pages={113-22}
}
The solution structure and the mode of action of arenicin isoform 1, an antimicrobial peptide with a unique 18-residue loop structure, from the lugworm Arenicola marina were elucidated here. Arenicin folds into a two-stranded antiparallel beta-sheet. It exhibits high antibacterial activity at 37 and 4 degrees C against Gram-negative bacteria, including polymyxin B-resistant Proteus mirabilis. Bacterial killing occurs within minutes and is accompanied by membrane permeabilization, membrane… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 33 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 30 references

Dissection of the mechanisms of cytolytic and antibacterial activity of lysenin, a defence protein of the annelid

  • J. Andrä, H. others 5 Bruhn, J. Winkelmann, C. Andersen, M. Leippe
  • 2006

Similar Papers

Loading similar papers…