Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: implications for a novel mechanism of action.

@article{Zhao2006InteractionOT,
  title={Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: implications for a novel mechanism of action.},
  author={Hongxia Zhao and Rohit Sood and Arimatti Jutila and Shambhunath Bose and Gunnar Fimland and Jon Nissen-Meyer and Paavo K. J. Kinnunen},
  journal={Biochimica et biophysica acta},
  year={2006},
  volume={1758 9},
  pages={1461-74}
}
Plantaricin A (plA) is a 26-residue bacteria-produced peptide pheromone with membrane-permeabilizing antimicrobial activity. In this study the interaction of plA with membranes is shown to be highly dependent on the membrane lipid composition. PlA bound readily to zwitterionic 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine (SOPC) monolayers and liposomes, yet without significantly penetrating into these membranes. The presence of cholesterol attenuated the intercalation of plA into SOPC… CONTINUE READING

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