Permeabilizing action of an antimicrobial lactoferricin-derived peptide on bacterial and artificial membranes.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Aguilera O,Ostolaza H,Quirós LM,Fierro JF

doi

10.1016/s0014-5793(99)01545-8

keywords:

subject

Has Abstract

pub_date

1999-12-03 00:00:00

pages

273-7

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(99)01545-8

journal_volume

462

pub_type

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