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Structure and mode of action of the antimicrobial peptide arenicin

2008; Portland Press; Volume: 410; Issue: 1 Linguagem: Inglês

10.1042/bj20071051

1470-8728

Jörg Andrä, Igor Jakovkin, Joachim Grötzinger, Oliver Hecht, Anna D. Krasnosdembskaya, Torsten Goldmann, Thomas Gutsmann, Matthias Leippe,

Aquaculture disease management and microbiota

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.