Solid-state NMR investigations of membrane-associated antimicrobial peptides.

Abstract

Solid-state NMR and other biophysical investigations have revealed many mechanistic details about the interactions of antimicrobial peptides with membranes. These studies have shaped our view on how these peptides cause the killing of bacteria, fungi, or tumour cells and how they permeabilize model membranes. As a result, we better understand the biological activities of these peptides and we are now able to design new and better sequences. Here we present some of the tools that have allowed these solid-state NMR investigations, including detailed protocols on how to reconstitute the peptides into oriented or non-oriented membranes as well as simple set-up procedures for (2)H as well as proton-decoupled (31)P or (15)N solid-state NMR measurements. Static and magic angle spinning experiments are described. Where adequate, the special requirements for or limitations of some of the measurements are discussed. Solid-state NMR spectra of both lipids and peptides have been recorded, and through the ensemble of measurements a detailed picture of these complex peptide-lipid supramolecular systems has finally emerged.