Interaction of the pore forming-peptide antibiotics Pep 5, nisin and subtilin with non-energized liposomes

• Published in: FEBS letters Vol. 244; no. 1; pp. 99 - 102
• Main Authors: Kordel, Marianne, Schüller, Friederike, Sahl, Hans-G.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 13.02.1989
• Subjects: Anti-Bacterial Agents; antibiotics; Bacterial Proteins; Bacteriocins; Cationic peptide antibiotic; Cell Membrane - drug effects; Cell Membrane - physiology; CF, carboxyfluorescein; DMPC, dimyristoylphosphatidylcholine; DMPS, dimyristoylphosphatidylserine; DOPC, dioleoylphosphatidylcholine; DPA, dipicolinic acid; Fluoresceins - metabolism; Liposomes - metabolism; Melitten - pharmacology; Membrane Fluidity - drug effects; Membrane Fusion - drug effects; Membrane interaction; Membrane Potentials; Nisin; Nisin - metabolism; Nisin - pharmacology; PDA, pyrenedecanoic acid; Pep 5; Peptides - metabolism; Peptides - pharmacology; Peptides, Cyclic - metabolism; Peptides, Cyclic - pharmacology; pores; PS, phosphatidylserine; Spectrometry, Fluorescence; Subtilin; Temperature; tempol, 2,2,6,6-tetramethyl-4-piperidinole 1-oxide; Tes, 2- {[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]amino} ethanesulphonic acid; Tryptophan - analysis; Nisin; CF, carboxyfluorescein; tempol, 2,2,6,6-tetramethyl-4-piperidinole 1-oxide; Membrane interaction; Pep 5; Tes, 2- {[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]amino} ethanesulphonic acid; PS, phosphatidylserine; PDA, pyrenedecanoic acid; Subtilin; Cationic peptide antibiotic; DOPC, dioleoylphosphatidylcholine; DPA, dipicolinic acid; DMPC, dimyristoylphosphatidylcholine; DMPS, dimyristoylphosphatidylserine
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(89)81171-8

The cationic peptide antibiotics Pep 5, nisin and subtilin depolarize bacterial and artificial membranes by formation of voltage-dependent multi-state pores. Studies with non-energized liposomes indicated that the peptides do not span the membrane in the absence of a membrane potential. The effects of Pep 5 and nisin on neutral membranes, as studied by membrane fluidity, phase transition points and carboxyfluorescein efflux, were small compared to melittin. Acidic liposomes were affected more strongly, indicative of primarily electrostatic interactions with phospholipid head groups. Subtilin may slightly enter the hydrophobic core as suggested by tryptophan fluorescence quenching and liposome fusion experiments.