Membrane interactions of designed cyclic RW peptides by solid-state NMR spectroscopy
Year: 2026
Type: article
Abstract: Antimicrobial peptides (AMPs) are hoped to complement classical antibiotics in view of increasing microbial resistance. We investigate two members of a family of designed cyclic AMPs with different activity and selectivity. The cyclic hexapeptides are rich in arginine and tryptophan and have been shown previously to target cell membranes and to affect model membranes differently depending on the lipid membrane composition. To better understand their mechanisms of membrane perturbation, we investigated the interactions of cyclic RRRWWW and cyclic RWRWRW with various model membranes containing lipids commonly found in either bacterial or eukaryotic membranes. Using 31 P and 2 H solid-state NMR methods, we systematically analyzed the interactions between the peptides and lipid membranes at the molecular level. When POPE/POPG model membranes are investigated the two peptides exhibit distinct interactions with the PE and PG components, reflected in a different decrease in lipid chain order parameters. This decrease in deuterium order parameters and deformation of the vesicle shapes indicate disturbance of the lipid membrane structure by the peptides. Our study provides new insights into the molecular mechanisms of AMP-membrane interactions and can contribute to the understanding and development of novel antimicrobial agents. • Membrane interactions of RW-cyclic hexapeptides were investigated by solid-state NMR. • Distinct interactions with the PE and PG components of PE/PG membranes are monitored. • The detailed arrangement of R and W has considerable influence on membrane disruption.
Language: English
Subfield: Microbiology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,870
Awards: G116629194, Polymerinduzierte endosomale Freisetzung für drug delivery: die mechanistische Verknüpfung von pHinduzierter Polymerbindung, Leakage, Fusion und anderem physikalischchemischen Membranverhalten, G1800105685, G1949054838, Par-delà les frontières, l'Université de Strasbourg, G2255650664, G2694206344, G2856181238, Engineering antibacterial cationic amphipathic peptidomimetics for targeting biofilm-embedded and intracellular bacteria, G471331628, Apolipoprotein AI Mimetic Peptide lipid Asemblies, Synergistic action of a photosensitizer and antimicrobial peptides for superbugs destruction, G7240651115
OpenAlex ID: W7133609978