Influence of the arrangement and secondary structure of melittin peptides on the formation and stability of toroidal pores.

@article{Irudayam2011InfluenceOT,
  title={Influence of the arrangement and secondary structure of melittin peptides on the formation and stability of toroidal pores.},
  author={Sheeba Jem Irudayam and Max L. Berkowitz},
  journal={Biochimica et biophysica acta},
  year={2011},
  volume={1808 9},
  pages={
          2258-66
        }
}
Melittin interactions with lipid bilayers and melittin formed pores are extensively studied to understand the mechanism of the toroidal pore formation. Early experimental studies suggested that melittin peptide molecules are anchored by their positively charged residues located next to the C-terminus to only one leaflet of the lipid bilayer (asymmetric arrangement). However, the recent non-linear spectroscopic experiment suggests a symmetric arrangement of the peptides with the C-terminus of… CONTINUE READING
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