The synergistic action of melittin and phospholipase A2 with lipid membranes: Development of linear dichroism for membrane-insertion kinetics

Angeliki Damianoglou, Alison Rodger, Catherine Pridmore, Timothy R. Dafforn, Jackie A. Mosely, John M. Sanderson, Matthew R. Hicks

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

Here we present data on the kinetics of insertion of melittin, a peptide from bee venom, into lipid membranes of different composition. Another component of bee venom is the enzyme phospholipase A2 (PLA 2). We have examined the interaction of melittin and PLA 2 with liposomes both separately and combined and demonstrate that they work synergistically to disrupt the membranes. A dramatic difference in the action of melittin and PLA 2 is observed when the composition of the membrane is altered. Temperature also has a large effect on the kinetics of insertion and membrane disruption. We use a combination of techniques to measure liposome size (dynamic light scattering), peptide secondary structure (circular dichroism spectroscopy), peptide orientation relative to the membrane (linear dichroism spectroscopy) and enzymatic digestion of the lipids (mass spectrometry).

Original languageEnglish
Pages (from-to)1351-1362
Number of pages12
JournalProtein and peptide letters
Volume17
Issue number11
Publication statusPublished - Nov 2010
Externally publishedYes

Keywords

  • Amphipathic
  • Antimicrobial
  • Dynamic light scattering
  • Linear dichroism
  • Liposome
  • Membrane protein
  • Peptide

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