Abstract
Molecular dynamics simulations of the polycationic antimicrobial peptide dendrimer (Leu)8(DapLeu)4(DapPhe)2DapLys-NH2 binding to membranes suggest that electrostatic interactions with the polyanionic lipopolysaccharide (LPS) and conformational flexibility of the 2,3-diaminopropanoic acid (Dap) branching units drive its selective insertion into microbial membranes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Infective Agents / chemistry
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Anti-Infective Agents / metabolism*
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Anti-Infective Agents / pharmacology
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Antimicrobial Cationic Peptides / chemistry
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Antimicrobial Cationic Peptides / metabolism*
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Antimicrobial Cationic Peptides / pharmacology
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Bacteria / drug effects
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Bacteria / metabolism*
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Dendrimers / chemistry
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Dendrimers / metabolism*
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Dendrimers / pharmacology
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Lipopolysaccharides / metabolism*
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Molecular Dynamics Simulation
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Static Electricity
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beta-Alanine / analogs & derivatives
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beta-Alanine / chemistry
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beta-Alanine / metabolism
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beta-Alanine / pharmacology
Substances
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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Dendrimers
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Lipopolysaccharides
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beta-Alanine
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2,3-diaminopropionic acid