PMID: 109121Apr 19, 1979

Interactions between bacterial membranes and peptidolipids: lysis of micrococcus luteus protoplasts by derivatives of peptidolipidic antibiotics from bacillus subtilis

Biochimica Et Biophysica Acta
F BessonG Michel

Abstract

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.

References

Sep 1, 1978·FEBS Letters·C Garbay-JaureguiberryG Michel
Apr 1, 1948·Proceedings of the Society for Experimental Biology and Medicine·M LANDY, G H WARREN

Related Concepts

Bacteriocidal Agents
Natto Bacteria
Plasma Membrane
Saturated Fat
Micrococcus
Oligopeptides
Cyclic Peptides
Protoplasts
Structure-Activity Relationship

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