Rational design of vector and antibiotic peptides using solid-state NMR.
The application of 2H solid-state NMR in determining structure activity relationships and mechanism of action of membrane active peptides is discussed. The enhancement of the disruption of anionic lipids in the membrane by new lead compounds is shown to be a key determinant of both DNA vector and antimicrobial activity.
Mason
A J
AJ
Faculté de Chimie, Université Louis Pasteur/ CNRS LC3-UMR7177, Institut le Bel, Strasbourg, France. jmason@chimie.u-strasbg.fr
Bechinger
B
B
Kichler
A
A
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology; D002462:Cell Membrane / Q000187:drug effects; D004247:DNA / Q000737:chemistry; D015195:Drug Design; D005822:Genetic Vectors / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D004247:DNA