| Abstract
| - Molecular dynamics simulations of the magainin MG-H2 peptide interacting with a modelphospholipid membrane have been used to investigate the mechanism by which antimicrobial peptidesact. Multiple copies of the peptide were randomly placed in solution close to the membrane. The peptidereadily bound to the membrane, and above a certain concentration, the peptide was observed tocooperatively induce the formation of a nanometer-sized, toroidally shaped pore in the bilayer. In sharpcontrast with the commonly accepted model of a toroidal pore, only one peptide was typically found nearthe center of the pore. The remaining peptides lay close to the edge of the pore, maintaining a predominantlyparallel orientation with respect to the membrane.
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