Molecular insight into mechanism of antimicrobial action of the β-hairpin peptide arenicin: Specific oligomerization in detergent micelles
✍ Scribed by Tatiana V. Ovchinnikova; Zakhar O. Shenkarev; Sergey V. Balandin; Kirill D. Nadezhdin; Alexander S. Paramonov; Vladimir N. Kokryakov; Alexander S. Arseniev
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2008
- Tongue
- English
- Volume
- 89
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Arenicins are 21‐residue cationic antimicrobial peptides isolated from marine polychaeta Arenicola marina. The peptides exhibit potent broad‐spectrum antimicrobial activity. In water solution arenicin‐2 adopts a β‐hairpin conformation, stabilized by one disulfide and nine hydrogen bonds. To determine the propensity for the peptide oligomerization in membrane mimetic systems, the recombinant arenicin‐2 was overexpressed as a fused form in Escherichia coli. The arenicin‐2 oligomerization and intermolecular packing in membrane mimicking environment were investigated using high‐resolution NMR spectroscopy. The present studies show that arenicin‐2 preserves a β‐hairpin structure and forms asymmetric dimers upon incorporation into the dodecylphosphocholine micelle. Two monomers of arenicin‐2 are aligned parallel to each other by the N‐terminal strands of the β‐hairpin (CN↑↑NC type of association). Polyacrylamide gel electrophoresis analysis indicated that in environment of anionic SDS micelles the arenicin‐2 might undergo further oligomerization and form tetramers. Our results afford further molecular insight into possible mechanism of antimicrobial action of arenicins. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 455–464, 2008.
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