Open AccessSusceptibility of bacterial, eukaryotic and artificial membranes to the disruptive action of the cationic peptides Pep 5 and nisin
Author(s) -
Kordel Marianne,
Sahl HansGeorg
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01393.x
Subject(s) - nisin , melittin , biochemistry , membrane , biology , peptide , bacteriocin , efflux , escherichia coli , chemistry , microbiology and biotechnology , antimicrobial , gene
The cationic bactericidal peptides Pep 5 and nisin render membranes permeable to low‐ M r compounds. All Gram‐positive bacteria treated with these peptides showed an immediate efflux of entrapped radioactive markers. The uptake of α‐[ 14 C]methylglucoside by the phosphoenolpyruvate‐dependent phosphotransferase system was stimulated by Pep 5, supporting previous results that pep 5 abolishes the membrane potential. Oxygen consumption was inhibited, presumably due to lack of ADP. Escherichia coli became sensitive to Pep 5 and nisin when the outer membrane was bypassed by osmotic shock or by formation of cytoplasmic membrane vesicles. In contrast, Mycoplasma cells and erythrocytes were unaffected by Pep 5 and nisin in concentrations up to 1 mM. Human lung fibroblasts released only small amounts of ATP when treated with Pep 5 and nisin in μM concentrations. Eukaryotic and Mycoplasma cells were disrupted more effectively by the bee venom peptide melittin, which displays overall structural similarities to Pep 5 and nisin. Various artificial membranes were not affected by Pep 5, nisin, or melittin.