Abstract
Host defence peptides (HDPs) are effector components of innate immunity that provide defence against pathogens. These are small-to-medium sized proteins which fold into amphipathic conformations toxic to microbial membranes. Here we explore the concept of supramolecular amphipathicity for probing antimicrobial propensity of HDPs using elementary HDP-like amphiphiles. Such amphiphiles are individually inactive, but when ordered into microscopic micellar assemblies, respond to membrane binding according to the orthogonal type of their primary structure. The study demonstrates that inducible supramolecular amphipathicity can discriminate against bacterial growth and colonisation thereby offering a physico-chemical rationale for tuneable targeting of biological membranes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Anti-Bacterial Agents / chemical synthesis
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / pharmacology*
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Antimicrobial Cationic Peptides / chemical synthesis
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Antimicrobial Cationic Peptides / chemistry*
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Antimicrobial Cationic Peptides / pharmacology*
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Cattle
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Dose-Response Relationship, Drug
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Erythrocytes / drug effects
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Escherichia coli / cytology
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Escherichia coli / drug effects*
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Escherichia coli / growth & development
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Hemolysis / drug effects
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Humans
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Microbial Sensitivity Tests
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Pseudomonas aeruginosa / cytology
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Pseudomonas aeruginosa / drug effects*
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Pseudomonas aeruginosa / growth & development
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Staphylococcus aureus / cytology
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Staphylococcus aureus / drug effects*
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Staphylococcus aureus / growth & development
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Structure-Activity Relationship
Substances
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides