Permeabilizing action of an antimicrobial lactoferricin-derived peptide on bacterial and artificial membranes.
A synthetic peptide (23 residues) that includes the antibacterial and lipopolysaccharide-binding regions of human lactoferricin, an antimicrobial sequence of lactoferrin, was used to study its action on cytoplasmic membrane of Escherichia coli 0111 and E. coli phospholipid vesicles. The peptide caused a depolarization of the bacterial cytoplasmic membrane, loss of the pH gradient, and a bactericidal effect on E. coli. Similarly, the binding of the peptide to liposomes dissipated previously created transmembrane electrical and pH gradients. The dramatic consequences of the transmembrane ion flux during the peptide exposure indicate that the adverse effect on bacterial cells occurs at the bacterial inner membrane.
Aguilera
O
O
Laboratory of Oral Microbiology, School of Stomatology, Oviedo, Spain.
Ostolaza
H
H
Quirós
L M
LM
Fierro
J F
JF
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D004594:Electrophysiology; D004926:Escherichia coli / Q000737:chemistry / Q000254:growth & development / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D007781:Lactoferrin / Q000031:analogs & derivatives* / Q000494:pharmacology*; D008081:Liposomes / Q000187:drug effects / Q000378:metabolism; D008564:Membrane Potentials / Q000187:drug effects; D008567:Membranes, Artificial; D010539:Permeability / Q000187:drug effects; D011485:Protein Binding / Q000187:drug effects; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D014364:Tryptophan / Q000378:metabolism; D014634:Valinomycin / Q000494:pharmacology
D000900:Anti-Bacterial Agents; C403330:Lfpep peptide; D008081:Liposomes; D008567:Membranes, Artificial; D014634:Valinomycin; D014364:Tryptophan; D007781:Lactoferrin