A membrane perspective on peptide-membrane interactions: recent results from solid-state NMR

While solid-state NMR has become renowned over the past three decades for its ability to study membrane and fibrillar proteins in their native states, determine high-resolution 3D structures, and identify docking sites between proteins and ligands, most studies have focused on the protein perspective by using isotopically labeled proteins. More recently, lipid-protein interactions are increasingly being examined from the lipid perspective, utilizing lipids and fatty acids, either isotopically labeled or unlabeled. In parallel, the development of in vivo solid-state NMR now enables the adoption of this approach within cellular membrane contexts, particularly in live bacteria. Here, we present examples utilizing ²H, ³¹P, ¹³C, ¹⁵N, ¹H and ¹⁹F NMR, with special emphasis on experiments conducted on bacteria or model membranes comprising bacterial lipids. Beyond the technological advancements, this approach enables the investigation of the molecular mechanisms of action of antimicrobial peptides, an area of crucial importance for the development of effective therapeutics.