Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides.

  title={Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides.},
  author={Jascindra Ravi and Angelo Bella and Ana Jo{\~a}o V Correia and Baptiste Lamarre and Maxim G. Ryadnov},
  journal={Physical chemistry chemical physics : PCCP},
  volume={17 24},
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… 

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