Structure and membrane interactions of chionodracine, a piscidin-like antimicrobial peptide from the icefish Chionodraco hamatus

Cristina Olivieri, Francesco Buonocore, Simona Picchietti, Anna Rita Taddei, Chiara Bernini, Giuseppe Scapigliati, Alysha A. Dicke, Vitaly V. Vostrikov, Gianluigi Veglia, Fernando Porcelli

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Abstract Chionodracine (Cnd) is a 22-residue peptide of the piscidin family expressed in the gills of the Chionodraco hamatus as protection from bacterial infections. Here, we report the effects of synthetic Cnd on both Psychrobacter sp. TAD1 and Escherichia coli bacteria, as well as membrane models. We found that Cnd perforates the inner and outer membranes of Psychrobacter sp. TAD1, making discrete pores that cause the cellular content to leak out. Membrane disruption studies using intrinsic and extrinsic fluorescence spectroscopy revealed that Cnd behaves similarly to other piscidins, with comparable membrane partition coefficients. Membrane accessibility assays and structural studies using NMR in detergent micelles show that Cnd adopts a canonical topology of antimicrobial helical peptides, with the hydrophobic face toward the lipid environment and the hydrophilic face toward the bulk solvent. The analysis of Cnd free energy of binding to vesicles with different lipid contents indicates a preference for charged phospholipids and a more marked binding to native E. coli extracts. Taken with previous studies on piscidin-like peptides, we conclude that Cnd first adsorbs to the membrane, and then forms pores together with membrane fragmentation. Since Cnd has only marginal hemolytic activity, it constitutes a good template for developing new antimicrobial agents.

Original languageEnglish (US)
Article number81836
Pages (from-to)1285-1293
Number of pages9
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1848
Issue number6
DOIs
StatePublished - Jun 2015

Keywords

  • Antimicrobial peptides
  • Fluorescence
  • Membrane permeabilization
  • NMR
  • Piscidins
  • Structure

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