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Action of Antimicrobial Peptides: Two-State Model†
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Section:Abstract
The argument and experimental evidence are presented for a two-state model that explains the action of both helical and β-sheet antimicrobial peptides after they bind to the plasma membranes of cells. Each peptide has two distinct physical states of binding to lipid bilayers. At low peptide-to-lipid ratios (P/L), the peptide tends to adsorb in the lipid headgroup region in a functionally inactive state. At a P/L above a threshold value P/L*, the peptide forms a multiple-pore state that is lethal to a cell. The susceptibility of a cell to an antimicrobial peptide depends on the value of P/L* that is determined by the lipid composition of the cell membrane. This model provides plausible explanations for the experimental findings that the susceptibility of different bacteria to a peptide is not directly correlated to its binding affinity, different peptides preferentially kill different pathogens, and peptides exhibit varying levels of lytic activity against different eukaryotic cells.
Citing Articles
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This article has been cited by 68 ACS Journal articles (5 most recent appear below).
Obstacles and Solutions to the Use of Cationic Antimicrobial Peptides in the Treatment of Cancer
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Ashley L. HilchieMelanie R. Power CoombsDavid W. Hoskin2012 (), 61-78Cationic antimicrobial peptides (CAPs) are cytotoxic agents that show promise for use in conjunction with current anti-cancer therapies to improve the specific killing of cancer cells. CAPs are small peptides that constitute an important innate defense ...
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Kathleen F. Wang, Ramanathan Nagarajan, Charlene M. Mello, and Terri A. CamesanoThe Journal of Physical Chemistry B2011 115 (51), 15228-15235Antimicrobial peptides (AMPs) are naturally occurring polymers that can kill bacteria by destabilizing their membranes. A quartz crystal microbalance with dissipation monitoring (QCM-D) was used to better understand the action of the AMP chrysophsin-3 on ...
Using Infrared Spectroscopy of Cyanylated Cysteine To Map the Membrane Binding Structure and Orientation of the Hybrid Antimicrobial Peptide CM15
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Katherine N. Alfieri, Alice R. Vienneau, and Casey H. LonderganBiochemistry2011 50 (51), 11097-11108The synthetic antimicrobial peptide CM15, a hybrid of N-terminal sequences from cecropin and melittin peptides, has been shown to be extremely potent. Its mechanism of action has been thought to involve pore formation based on prior site-directed spin ...
Jointly Handling Potency and Toxicity of Antimicrobial Peptidomimetics by Simple Rules from Desirability Theory and Chemoinformatics
Maykel Cruz-Monteagudo, Fernanda Borges, and M. Natália D. S. CordeiroJournal of Chemical Information and Modeling2011 51 (12), 3060-3077Jointly Handling Potency and Toxicity of Antimicrobial Peptidomimetics by Simple Rules from Desirability Theory and Chemoinformatics
Maykel Cruz-Monteagudo, Fernanda Borges, and M. Natália D. S. CordeiroJournal of Chemical Information and Modeling2011 51 (12), 3060-3077Today, emerging and increasing resistance to antibiotics has become a threat to public health worldwide. Antimicrobial peptides have unique action mechanisms making them an attractive therapeutic prospect to be applied against resistant bacteria. However, ...
Effect of Cholesterol on the Membrane Interaction of Modelin-5 Isoforms
Sarah R. Dennison and David A. PhoenixBiochemistry2011 50 (50), 10898-10909Effect of Cholesterol on the Membrane Interaction of Modelin-5 Isoforms
Sarah R. Dennison and David A. PhoenixBiochemistry2011 50 (50), 10898-10909Modelin-5 isoforms were used to gain an insight into the effects of amidation on antimicrobial selectivity. When tested against Escherichia coli, amidation increased toxicity 10-fold (MIC = 31.25 μM) while showing limited increased hemolytic activity (2% ...
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History
- Published In Issue July 25, 2000
- Received April 25, 2000
Revised Manuscript Received May 26, 2000
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