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

FEBS Letters

Ostolaza, H.¹  Quirós, L.M.²  Fierro, J.F.³  Aguilera, O.³ 

[1] Unit of Biophysic (CSIC-UPV/EHU) and Department of Biochemistry, University of the Basque Country, 48080 Bilbao, Spain;Department of Functional Biology (Microbiology), Faculty of Medicine, University of Oviedo, C/Julián Claverı́a, s.n., 33006 Oviedo, Spain;Laboratory of Oral Microbiology, School of Stomatology, Oviedo, Spain

关键词: Lactoferricin;    Lactoferrin;    Liposome;    Antimicrobial peptide;    Escherichia coli;    ANTS;    8-aminonaphthalene-1;    3;    6-trisulfonic acid;    DPX;    p-xylene-bis-pyridiniumbromide;    diS-C3-(5);    3;    3′-dipropylthiadicarbocyanine iodide;    K-PIPES;    potassium piperazine-N;    N′-bis-(ethanosulfonate);    Pyranine;    8-hydroxypyrene-1;    3;    6-trisulfonic acid trisodium salt;    [3H]TPP+;    [3H]-tetraphenylphosphonium bromide;   

DOI  :  10.1016/S0014-5793(99)01545-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown