TAILIEUCHUNG - Báo cáo khoa học: The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes

Peptides composed of leucyl and lysyl residues ( LK pep-tides ) with different compositions and sequences were compared for their antibacterial activities usingcell wall-less bacteria of the classMollicutes(acholeplasmas, mycoplas-mas and spiroplasmas) as targets. The antibacterial activity of the amphipathica-helical peptides varied with their size, 15 residues beingthe optimal length, independent of the membrane hydrophobic core thickness and the amount of cholesterol. | Eur. J. Biochem. 270 2207-2217 2003 FEBS 2003 doi The antibiotic activity of cationic linear amphipathic peptides lessons from the action of leucine lysine copolymers on bacteria of the class Mollicutes Laure Beven1 Sabine Castano2 Jean Dufourcq2 AAke Wieslander3 and Henri Wroblewski1 1UMR CNRS 6026 Université de Rennes 1 France 2Centre de Recherche Paul Pascal CNRS Pessac France 3Department of Biochemistry and Biophysics Stockholm University Sweden Peptides composed of leucyl and lysyl residues LK peptides with different compositions and sequences were compared for their antibacterial activities using cell wall-less bacteria of the class Mollicutes acholeplasmas mycoplasmas and spiroplasmas as targets. The antibacterial activity of the amphipathic a-helical peptides varied with their size 15 residues being the optimal eeggth independent of die membrane hydrophobic core thickness and the amount of cholesterol. The 15-residue ideally amphipathic a helix with a 5 positive net charge KLLKLLLKLLLKLLK had the strongest antibacterial activity similar to that of melittin. In contrast scrambled peptides devoid of amphipathy and the less hydrophobic b-sheeted peptides LK nK even those 15-residue long were far less potent than the helical ones. Furthermore the growth inhibitory activity of the peptides was correlated with their ability to abolish membrane potential. These data are fully consistent with a predominantly flat orientation of LK peptides at the lipid water interface and strongly supports that these peptides and probably the linear polycationic amphipathic defence peptides act on bacterial membranes in four main steps according to the carpet model a interfacial partitioning with accumulation of monomers on the target membrane limiting tèeep th pep iide structural chanhes conformttiion. aggregation and orientation induced by interactions with the lipid bilayer as already shown with liposomes and erythrocytes c plasma membrane .

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