The synergistic action of melittin and phospholipase A2 with lipid membranes : development of linear dichroism for membrane-insertion kinetics
| Autor: | Alison Rodger, John M. Sanderson, Timothy R. Dafforn, Matthew R. Hicks, Catherine J. Pridmore, Jackie A. Mosely, Angeliki Damianoglou |
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| Rok vydání: | 2010 |
| Předmět: |
Circular dichroism
Protein Conformation Lipid Bilayers Peptide Biochemistry chemistry.chemical_compound Structural Biology chemistry.chemical_classification Liposome Crystallography biology Temperature Membrane General Medicine Bees (DOPC) Bee Venoms (TLC) DMPC Dynamic light scattering lipids (amino acids peptides and proteins) DOPG (PDPC) (OCD) Dynamic Glycerophospholipids Linear dichroism Linear complex mixtures Melittin Phospholipase A2 Animals POPC Spectrum Analysis Amphipathic Melitten (mass spectrometry) NMR Phospholipases A2 chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Membrane protein Liposomes biology.protein (LD) Antimicrobial (PLA2) (POPC) |
| Zdroj: | Protein & peptide letters, 2010, Vol.17(11), pp.1351-1362 ResearcherID |
| Popis: | 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). |
| Databáze: | OpenAIRE |
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