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Permeabilizing action of an antimicrobial lactoferricin‐derived peptide on bacterial and artificial membranes
Author(s) -
Aguilera O.,
Ostolaza H.,
Quirós L.M.,
Fierro J.F.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01545-8
Subject(s) - peptide , escherichia coli , lactoferrin , liposome , antimicrobial peptides , transmembrane protein , biochemistry , cytoplasm , membrane , chemistry , biophysics , peptide sequence , biology , receptor , gene
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.