A membrane perspective on peptide-membrane interactions: recent results from solid-state NMR
Abstract
While solid-state NMR has become renowned over the past three decades for its ability to study membrane and brillar 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 amino-acids. 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.
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BibTeX
@article{zaatouf2026membrane,
title = {{A membrane perspective on peptide-membrane interactions: recent results from solid-state NMR}},
author = {Laila Zaatouf and Hugo Legras-Hemonnot and Dror E Warschawski},
journal = {Biomedical journal},
year = {2026},
month = sep,
doi = {10.1016/j.bj.2025.100943},
url = {https://hal.science/hal-05760288v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - A membrane perspective on peptide-membrane interactions: recent results from solid-state NMR
AU - Laila Zaatouf
AU - Hugo Legras-Hemonnot
AU - Dror E Warschawski
PY - 2026
DA - 2026/09/30
JO - Biomedical journal
DO - 10.1016/j.bj.2025.100943
UR - https://hal.science/hal-05760288v1
AB - While solid-state NMR has become renowned over the past three decades for its ability to study membrane and brillar 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 amino-acids. 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.
SN - 2319-4170
SN - 2320-2890
ER -