The Synergistic Action of Melittin and Phospholipase A2 with Lipid Membranes: Development of Linear Dichroism for Membrane-Insertion Kinetics

Author(s): Angeliki Damianoglou, Alison Rodger, Catherine Pridmore, Timothy R. Dafforn, Jackie A. Mosely, John M. Sanderson, Matthew R. Hicks

Journal Name: Protein & Peptide Letters

Volume 17 , Issue 11 , 2010

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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 (PLA2). We have examined the interaction of melittin and PLA2 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 PLA2 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).

Keywords: Amphipathic, peptide, antimicrobial, membrane protein, linear dichroism, liposome, dynamic light scattering, membrane, linear, dynamic, (PLA2), (mass spectrometry), crystallography, NMR, (LD), Melittin, (DOPC), DOPG, (POPC), DMPC, (TLC), (OCD), (PDPC), EDTA, (DHB), MALDI, Spectroscopy, CD222/CD208, PA2, FTIR analysis

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Article Details

Year: 2010
Page: [1351 - 1362]
Pages: 12
DOI: 10.2174/0929866511009011351
Price: $65

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