Mechanisms of Peptide-Induced Pore Formation in Lipid Bilayers Investigated by Oriented <sup>31</sup>P Solid-State NMR Spectroscopy

Mechanisms of Peptide-Induced Pore Formation in Lipid Bilayers Investigated by Oriented <sup>31</sup>P Solid-State NMR Spectroscopy. Bertelsen, K., Dorosz, J., Hansen, S. K., Nielsen, N. C., & Vosegaard, T. PLoS ONE, 7(10):e47745, Public Library of Science, 1, 2012.

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There is a considerable interest in understanding the function of antimicrobial peptides (AMPs), but the details of their mode of action is not fully understood. This motivates extensive efforts in determining structural and mechanistic parameters for AMPâ€™s interaction with lipid membranes. In this study we show that oriented-sample ³¹P solid-state NMR spectroscopy can be used to probe the membrane perturbations and -disruption by AMPs. For two AMPs, alamethicin and novicidin, we observe that the majority of the lipids remain in a planar bilayer conformation but that a number of lipids are involved in the peptide anchoring. These lipids display reduced dynamics. Our study supports previous studies showing that alamethicin adopts a transmembrane arrangement without significant disturbance of the surrounding lipids, while novicidin forms toroidal pores at high concentrations leading to more extensive membrane disturbance.

@article{ mendeley_5381522041,
  isauthor = {1},
  abstract = {<p>There is a considerable interest in understanding the function
of antimicrobial peptides (AMPs), but the details of their mode of
action is not fully understood. This motivates extensive efforts
in determining structural and mechanistic parameters for AMPâ€™s
interaction with lipid membranes. In this study we show that oriented-sample
<sup>31</sup>P solid-state NMR spectroscopy can be used to probe
the membrane perturbations and -disruption by AMPs. For two AMPs,
alamethicin and novicidin, we observe that the majority of the lipids
remain in a planar bilayer conformation but that a number of lipids
are involved in the peptide anchoring. These lipids display reduced
dynamics. Our study supports previous studies showing that alamethicin
adopts a transmembrane arrangement without significant disturbance
of the surrounding lipids, while novicidin forms toroidal pores at
high concentrations leading to more extensive membrane disturbance.</p>},
  month = {1},
  added = {1356878263},
  year = {2012},
  isstarred = {0},
  id = {5381522041},
  discipline = {Chemistry},
  deletionpending = {0},
  title = {Mechanisms of Peptide-Induced Pore Formation in Lipid Bilayers Investigated by Oriented <sup>31</sup>P Solid-State NMR Spectroscopy},
  journal = {PLoS ONE},
  version = {1366110857},
  pmid = {23094079},
  number = {10},
  url_mendeley = {http://www.mendeley.com/c/5381522041/p/8351003/bertelsen-2012-mechanisms-of-peptide-induced-pore-formation-in-lipid-bilayers-investigated-by-oriented-sup31supp-solid-state-nmr-spectroscopy/},
  source_type = {article},
  isread = {1},
  author = {Kresten {Bertelsen} and Jerzy {Dorosz} and Sara Krogh {Hansen} and Niels Chr. {Nielsen} and Thomas {Vosegaard}},
  pages = {e47745},
  volume = {7},
  publisher = {Public Library of Science},
  doi = {10.1371/journal.pone.0047745},
  url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3475706&tool=pmcentrez&rendertype=abstract
http://dx.doi.org/10.1371/journal.pone.0047745},
  type = {Journal Article},
  issn = {1932-6203},
  modified = {1366110857},
  citation_key = {bertelsen2012},
  subdiscipline = {Nuclear Magnetic Resonance},
  journal = {PLoS ONE},
  dateaccessed = {24/03/13}
}

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