Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions.

@article{Rzepiela2010MembranePB,
  title={Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions.},
  author={Andrzej J. Rzepiela and Durba Sengupta and Nicolae Goga and Siewert J. Marrink},
  journal={Faraday discussions},
  year={2010},
  volume={144},
  pages={431-43; discussion 445-81}
}
Antimicrobial peptides (AMPs) comprise a large family of peptides that include small cationic peptides, such as magainins, which permeabilize lipid membranes. Previous atomistic level simulations of magainin-H2 peptides show that they act by forming toroidal transmembrane pores. However, due to the atomistic level of description, these simulations were necessarily limited to small system sizes and sub-microsecond time scales. Here, we study the long-time relaxation properties of these pores by… CONTINUE READING

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