Structure and mode of action of the antimicrobial peptide arenicin.

  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},
  volume={410 1},
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


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

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