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Issue 24, 2015
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Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides

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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.

Graphical abstract: Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides

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Article information


Submitted
27 Feb 2015
Accepted
30 Apr 2015
First published
06 May 2015

Phys. Chem. Chem. Phys., 2015,17, 15608-15614
Article type
Paper
Author version available

Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides

J. Ravi, A. Bella, A. J. V. Correia, B. Lamarre and M. G. Ryadnov, Phys. Chem. Chem. Phys., 2015, 17, 15608
DOI: 10.1039/C5CP01185J

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