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https://hdl.handle.net/2440/57828
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dc.contributor.author | Sherman, P. | - |
dc.contributor.author | Jackway, R. | - |
dc.contributor.author | Gehman, J. | - |
dc.contributor.author | Praporski, S. | - |
dc.contributor.author | McCubbin, G. | - |
dc.contributor.author | Mechler, A. | - |
dc.contributor.author | Martin, L. | - |
dc.contributor.author | Separovic, F. | - |
dc.contributor.author | Bowie, J. | - |
dc.date.issued | 2009 | - |
dc.identifier.citation | Biochemistry, 2009; 48(50):11892-11901 | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.issn | 1520-4995 | - |
dc.identifier.uri | http://hdl.handle.net/2440/57828 | - |
dc.description | Copyright © 2009 American Chemical Society | - |
dc.description.abstract | The solution structure of fallaxidin 4.1a, a C-terminal amidated analogue of fallaxidin 4.1, a cationic antimicrobial peptide isolated from the amphibian Litoria fallax, has been determined by nuclear magnetic resonance (NMR). In zwitterionic dodecylphosphocholine (DPC) micelles, fallaxidin 4.1a adopted a partially helical structure with random coil characteristics. The flexibility of the structure may enhance the binding and penetration upon interaction with microbial membranes. Solid-state (31)P and (2)H NMR was used to investigate the effects of fallaxidin 4.1a on the dynamics of phospholipid membranes, using acyl chain deuterated zwitterionic dimyristoylphosphatidylcholine (DMPC-d(54)) and anionic dimyristoylphosphatidylglycerol (DMPG) multilamellar vesicles. In DMPC-d(54) vesicle bilayers, fallaxidin 4.1a caused a decrease in the (31)P chemical shift anisotropy (CSA), and a decrease in deuterium order parameters from the upper acyl chain region, indicating increased lipid motion about the phosphate headgroups. Conversely, for DMPC-d(54)/DMPG, two (31)P CSA were observed due to a lateral phase separation of the two lipids and/or differing headgroup orientations in the presence of fallaxidin 4.1a, with a preferential interaction with DMPG. Little effect on the deuterated acyl chain order parameters was observed in the d(54)-DMPC/DMPG model membranes. Real time quartz crystal microbalance analyses of fallaxidin 4.1a addition to DMPC and DMPC/DMPG supported lipid bilayers together with the NMR results indicated transmembrane pore formation in DMPC/DMPG membranes and peptide insertion followed by disruption at a threshold concentration in DMPC membranes. The different interactions observed with "mammalian" (DMPC) and "bacterial" (DMPC/DMPG) model membranes imply fallaxidin 4.1a may be a useful antimicrobial peptide, with preferential cytolytic activity toward prokaryotic organisms at low peptide concentrations (<5 microM). | - |
dc.description.statementofresponsibility | Patrick J. Sherman, Rebecca J. Jackway, John D. Gehman, Slavica Praporski, George A. McCubbin, Adam Mechler, Lisandra L. Martin, Frances Separovic and John H. Bowie | - |
dc.language.iso | en | - |
dc.publisher | Amer Chemical Soc | - |
dc.source.uri | http://dx.doi.org/10.1021/bi901668y | - |
dc.subject | Cell Membrane | - |
dc.subject | Animals | - |
dc.subject | Anura | - |
dc.subject | Gram-Positive Bacteria | - |
dc.subject | Quartz | - |
dc.subject | Lipid Bilayers | - |
dc.subject | Dimyristoylphosphatidylcholine | - |
dc.subject | Antimicrobial Cationic Peptides | - |
dc.subject | Solutions | - |
dc.subject | Crystallization | - |
dc.subject | Nuclear Magnetic Resonance, Biomolecular | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Molecular Sequence Data | - |
dc.title | Solution structure and membrane interactions of the antimicrobial peptide Fallaxidin 4.1a: An NMR and QCM study | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1021/bi901668y | - |
pubs.publication-status | Published | - |
Appears in Collections: | Aurora harvest 5 Biochemistry publications |
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