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• W2041501639 endingPage "11901" @default.
• W2041501639 startingPage "11892" @default.
• W2041501639 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 31P and 2H NMR was used to investigate the effects of fallaxidin 4.1a on the dynamics of phospholipid membranes, using acyl chain deuterated zwitterionic dimyristoylphosphatidylcholine (DMPC-d54) and anionic dimyristoylphosphatidylglycerol (DMPG) multilamellar vesicles. In DMPC-d54 vesicle bilayers, fallaxidin 4.1a caused a decrease in the 31P 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-d54/DMPG, two 31P 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 d54-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 μM)." @default.
• W2041501639 created "2016-06-24" @default.
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• W2041501639 date "2009-11-13" @default.
• W2041501639 modified "2023-10-18" @default.
• W2041501639 title "Solution Structure and Membrane Interactions of the Antimicrobial Peptide Fallaxidin 4.1a: An NMR and QCM Study" @default.
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• W2041501639 doi "https://doi.org/10.1021/bi901668y" @default.
• W2041501639 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19894755" @default.
• W2041501639 hasPublicationYear "2009" @default.
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