Temperature-dependent transmembrane insertion of the amphiphilic peptide PGLa in lipid bilayers observed by solid state 19F NMR spectroscopy.

@article{Afonin2008TemperaturedependentTI,
  title={Temperature-dependent transmembrane insertion of the amphiphilic peptide PGLa in lipid bilayers observed by solid state 19F NMR spectroscopy.},
  author={Sergii Afonin and Stephan L. Grage and Marco Ieronimo and Parvesh Wadhwani and Anne S Ulrich},
  journal={Journal of the American Chemical Society},
  year={2008},
  volume={130 49},
  pages={16512-4}
}
Crucial for the activity of many antimicrobial peptides is their interaction with the lipid membrane of the target cell. To characterize this interaction, we studied the membrane-alignment of the R-helical amphiphilic antimicrobial peptide PGLa (GMASKAGAIAGKIAKVALKAL-amide) in DMPC/DMPG bilayers using solid state 19F NMR. Here, it is demonstrated that the helix alignment depends not only on peptide concentration, but that it changes even more dramatically with the temperature and lipid phase… CONTINUE READING

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