Structure and mode of action of the antimicrobial peptide arenicin

Biochem J. 2008 Feb 15;410(1):113-22. doi: 10.1042/BJ20071051.

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 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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / pharmacology*
  • Antimicrobial Cationic Peptides
  • Helminth Proteins
  • Hemolysis / drug effects
  • Humans
  • Lipid Bilayers
  • Magnetic Resonance Spectroscopy
  • Microbial Sensitivity Tests
  • Microscopy, Atomic Force
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / pharmacology*
  • Structure-Activity Relationship

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Helminth Proteins
  • Lipid Bilayers
  • Peptides
  • arenicin-1, Arenicola marina