Structure and mode of action of the antimicrobial peptide arenicin

Jörg Andrä*, Igor Jakovkin, Joachim Grötzinger, Oliver Hecht, Anna Krasnodembskaya, Torsten Goldmann, Thomas Gutsmann, Matthias Leippe

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

78 Citations (Scopus)

Abstract

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 β-sheet. It exhibits high antibacterial activity at 37 and 4°C against Gram-negative bacteria, including polymyxin B-resistant Proteus mirabilis. Bacterial killing occurs within minutes and is accompanied by membrane permeabilization, membrane detachment and release of cytoplasm. Interaction of arenicin with reconstituted membranes that mimic the lipopolysaccharide-containing outer membrane or the phospholipid-containing plasma membrane of Gram-negative bacteria exhibited no pronounced lipid specificity. Arenicin-induced current fluctuations in planar lipid bilayers correspond to the formation of short-lived heterogeneously structured lesions. Our results strongly suggest that membrane interaction plays a pivotal role in the antibacterial activity of arenicin.

Original languageEnglish
Pages (from-to)113-122
Number of pages10
JournalBiochemical Journal
Volume410
Issue number1
DOIs
Publication statusPublished - 15 Feb 2008

Keywords

  • Antimicrobial peptide
  • Atomic force microscopy (AFM)
  • Epithelial defence
  • Lipopolysaccharide (LPS)
  • Membrane permeabilization
  • Planar lipid bilayer

ASJC Scopus subject areas

  • Biochemistry

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