Antimicrobial peptides in action

Leontiadou, H., Mark, A. E. and Marrink, S. J. (2006) Antimicrobial peptides in action. Journal of The American Chemical Society, 128 37: 12156-12161. doi:10.1021/ja062927q


Author Leontiadou, H.
Mark, A. E.
Marrink, S. J.
Title Antimicrobial peptides in action
Journal name Journal of The American Chemical Society   Check publisher's open access policy
ISSN 0002-7863
Publication date 2006-01-01
Sub-type Article (original research)
DOI 10.1021/ja062927q
Volume 128
Issue 37
Start page 12156
End page 12161
Total pages 6
Place of publication Washington
Publisher Amer Chemical Soc
Collection year 2006
Language eng
Subject C1
780103 Chemical sciences
250699 Theoretical and Computational Chemistry not elsewhere classified
060112 Structural Biology (incl. Macromolecular Modelling)
0307 Theoretical and Computational Chemistry
Abstract Molecular dynamics simulations of the magainin MG-H2 peptide interacting with a model phospholipid membrane have been used to investigate the mechanism by which antimicrobial peptides act. Multiple copies of the peptide were randomly placed in solution close to the membrane. The peptide readily bound to the membrane, and above a certain concentration, the peptide was observed to cooperatively induce the formation of a nanometer- sized, toroidally shaped pore in the bilayer. In sharp contrast with the commonly accepted model of a toroidal pore, only one peptide was typically found near the center of the pore. The remaining peptides lay close to the edge of the pore, maintaining a predominantly parallel orientation with respect to the membrane.
Keyword Chemistry, Multidisciplinary
Molecular-dynamics Simulations
Pore Formation
Lipid-bilayers
Phospholipid-bilayers
Amphipathic Peptides
Membrane
Magainin
Orientation
Insertion
Analog
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 18:25:52 EST