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Solid-State NMR Studies of the Interactions and Structure of Antimicrobial Peptides in Model Membranes

  • Matthieu Fillion
  • Marise Ouellet
  • Michéle Auger
Reference work entry

Abstract

Cationic antimicrobial peptides are part of the innate immune system of several organisms and represent great hope to fight against multidrug-resistant bacteria. Despite their structural diversity, they share common characteristics such as a short length, a net positive charge, and an amphiphilic character. However, the detailed mechanisms of action of these peptides are still unclear. In the literature, there is clear evidence that cationic antimicrobial peptides target the membrane of bacterial pathogens where they induce defects that will eventually kill bacteria by creating an electrochemical gradient imbalance. Therefore, to design more potent and selective antimicrobial peptides that are viable on a pharmacological point of view, a better understanding of the molecular determinants involved in the membrane interactions is required.

In this regard, the most suitable technique to study cationic antimicrobial peptides in their native environment, i.e., a lipid bilayer in a fluid phase, is solid-state NMR. Exploiting the different NMR interactions, this technique has proven to be useful to provide information on the mutual interactions between membrane-active peptides and phospholipids with an atomic-scale resolution. In particular, the conformation of the peptides in addition to their location in the membrane is an important feature of the mechanism of action that needs to be addressed. In this context, this chapter is devoted to present the most recent developments in the field of solid-state NMR for elucidating the conformation and membrane topology of these peptides reconstituted in lipid mimetic membranes.

Keywords

Antimicrobial peptides Lipid membranes Solid-state NMR Interactions Structure Topology Dynamics Modes of action Degree of penetration Bacteria 

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Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  • Matthieu Fillion
    • 1
  • Marise Ouellet
    • 1
  • Michéle Auger
    • 1
  1. 1.Department of Chemistry, Regroupement québécois de recherche sur la fonction, l’ingénierie et les applications des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF)Université LavalQuébecCanada

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