Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides.
Phys Chem Chem Phys
; 17(24): 15608-14, 2015 Jun 28.
Article
em En
| MEDLINE
| ID: mdl-25966444
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pseudomonas aeruginosa
/
Staphylococcus aureus
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Peptídeos Catiônicos Antimicrobianos
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Escherichia coli
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Antibacterianos
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article