Abstract
We have studied the interaction of beta-17, a potent synthetic antimicrobial beta-peptide, with phospholipids. We find that unlike other antimicrobial peptides such as magainin II, beta-17 facilitates the formation of nonbilayer phases, indicating that the peptide promotes negative curvature. Studies of liposomal leakage also indicate a different mode of membrane interaction relative to magainin II, but both leakage and membrane binding show that beta-17, like magainin II, has strong affinity for membranes containing anionic lipids. This is likely to be an important factor contributing to the antimicrobial specificity of the beta-peptide.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / metabolism
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Anti-Infective Agents / chemistry*
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Anti-Infective Agents / metabolism
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Antimicrobial Cationic Peptides / chemistry*
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Antimicrobial Cationic Peptides / metabolism
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Calorimetry, Differential Scanning
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Cell Membrane / chemistry*
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Cell Membrane / metabolism
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Circular Dichroism
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Humans
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Lipid Bilayers / chemistry
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Lipid Bilayers / metabolism
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Molecular Structure
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Phospholipids / chemistry*
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Phospholipids / metabolism
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Protein Binding
Substances
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Anti-Bacterial Agents
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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Lipid Bilayers
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Phospholipids