Interactions between bacterial membranes and peptidolipids: lysis of micrococcus luteus protoplasts by derivatives of peptidolipidic antibiotics from bacillus subtilis.
The lysis of protoplasts of Micrococcus luteus has been tested with various derivatives of three peptidolipidic antibiotics: iturin A, mycosubtilin and bacillomycin L. The lytic activity is dependent to the nature of the substituting group and to the position of the substituted aminoacid residue. The acetylation of OH groups leads to a decrease of the lytic activity of the natural antibiotics. The methylation of aspartyl residues of bacillomycin L gives a strong lytic activity while natural bacillomycin L has no lytic activity. The methylation of the tyrosyl residue enhances the lytic activities of iturin A and of bacillomycin L-dimethyl ester and reduces that of mycosubtilin. Correlations between the structures of derivatives and their lytic action on M. luteus protoplasts are discussed.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001412:Bacillus subtilis; D002462:Cell Membrane / Q000187:drug effects / Q000648:ultrastructure*; D005227:Fatty Acids; D008837:Micrococcus / Q000648:ultrastructure*; D009842:Oligopeptides / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000494:pharmacology*; D011523:Protoplasts / Q000187:drug effects / Q000648:ultrastructure*; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D005227:Fatty Acids; D009842:Oligopeptides; D010456:Peptides, Cyclic