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Bactericidal activity of amphipathic cationic antimicrobial peptides involves altering the membrane fluidity when interacting with the phospholipid bilayer. / Omardien, Soraya; Drijfhout, Jan W.; Vaz, Frédéric M. et al.

In: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, Vol. 1860, No. 11, 2018, p. 2404-2415.

Research output: Contribution to journal › Article › Academic › peer-review

Harvard

Omardien, S, Drijfhout, JW, Vaz, FM, Wenzel, M, Hamoen, LW, Zaat, SAJ & Brul, S 2018, 'Bactericidal activity of amphipathic cationic antimicrobial peptides involves altering the membrane fluidity when interacting with the phospholipid bilayer', BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, vol. 1860, no. 11, pp. 2404-2415. https://doi.org/10.1016/j.bbamem.2018.06.004

APA

Omardien, S., Drijfhout, J. W., Vaz, F. M., Wenzel, M., Hamoen, L. W., Zaat, S. A. J., & Brul, S. (2018). Bactericidal activity of amphipathic cationic antimicrobial peptides involves altering the membrane fluidity when interacting with the phospholipid bilayer. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1860(11), 2404-2415. https://doi.org/10.1016/j.bbamem.2018.06.004

Vancouver

Omardien S, Drijfhout JW, Vaz FM, Wenzel M, Hamoen LW, Zaat SAJ et al. Bactericidal activity of amphipathic cationic antimicrobial peptides involves altering the membrane fluidity when interacting with the phospholipid bilayer. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES. 2018;1860(11):2404-2415. doi: 10.1016/j.bbamem.2018.06.004

Author

Omardien, Soraya ; Drijfhout, Jan W. ; Vaz, Frédéric M. et al. / Bactericidal activity of amphipathic cationic antimicrobial peptides involves altering the membrane fluidity when interacting with the phospholipid bilayer. In: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES. 2018 ; Vol. 1860, No. 11. pp. 2404-2415.

BibTeX

@article{2ecb134a12934f948e46e5ab114e3d08,
title = "Bactericidal activity of amphipathic cationic antimicrobial peptides involves altering the membrane fluidity when interacting with the phospholipid bilayer",
abstract = "Background: Amphipathic cationic antimicrobial peptides (AMPs) TC19 and TC84, derived from the major AMPs of human blood platelets, thrombocidins, and Bactericidal Peptide 2 (BP2), a synthetic designer peptide showed to perturb the membrane of Bacillus subtilis. We aimed to determine the means by which the three AMPs cause membrane perturbation in vivo using B. subtilis and to evaluate whether the membrane alterations are dependent on the phospholipid composition of the membrane. Methods: Physiological analysis was employed using Alexa Fluor 488 labelled TC84, various fluorescence dyes, fluorescent microscopy techniques and structured illumination microscopy. Results: TC19, TC84 and BP2 created extensive fluidity domains in the membrane that are permeable, thus facilitating the entering of the peptides and the leakage of the cytosol. The direct interaction of the peptides with the bilayer create the fluid domains. The changes caused in the packing of the phospholipids lead to the delocalization of membrane bound proteins, thus contributing to the cell's destruction. The changes made to the membrane appeared to be not dependent on the composition of the phospholipid bilayer. Conclusions: The distortion caused to the fluidity of the membrane by the AMPs is sufficient to facilitate the entering of the peptides and leakage of the cytosol. General significance: Here we show in vivo that cationic AMPs cause “membrane leaks” at the site of membrane insertion by altering the organization and fluidity of the membrane. Our findings thus contribute to the understanding of the membrane perturbation characteristic of cationic AMPs.",
author = "Soraya Omardien and Drijfhout, {Jan W.} and Vaz, {Fr{\'e}d{\'e}ric M.} and Michaela Wenzel and Hamoen, {Leendert W.} and Zaat, {Sebastian A. J.} and Stanley Brul",
year = "2018",
doi = "10.1016/j.bbamem.2018.06.004",
language = "English",
volume = "1860",
pages = "2404--2415",
journal = "BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES",
issn = "0005-2736",
publisher = "Elsevier",
number = "11",

}

RIS

TY - JOUR

T1 - Bactericidal activity of amphipathic cationic antimicrobial peptides involves altering the membrane fluidity when interacting with the phospholipid bilayer

AU - Omardien, Soraya

AU - Drijfhout, Jan W.

AU - Vaz, Frédéric M.

AU - Wenzel, Michaela

AU - Hamoen, Leendert W.

AU - Zaat, Sebastian A. J.

AU - Brul, Stanley

PY - 2018

Y1 - 2018

N2 - Background: Amphipathic cationic antimicrobial peptides (AMPs) TC19 and TC84, derived from the major AMPs of human blood platelets, thrombocidins, and Bactericidal Peptide 2 (BP2), a synthetic designer peptide showed to perturb the membrane of Bacillus subtilis. We aimed to determine the means by which the three AMPs cause membrane perturbation in vivo using B. subtilis and to evaluate whether the membrane alterations are dependent on the phospholipid composition of the membrane. Methods: Physiological analysis was employed using Alexa Fluor 488 labelled TC84, various fluorescence dyes, fluorescent microscopy techniques and structured illumination microscopy. Results: TC19, TC84 and BP2 created extensive fluidity domains in the membrane that are permeable, thus facilitating the entering of the peptides and the leakage of the cytosol. The direct interaction of the peptides with the bilayer create the fluid domains. The changes caused in the packing of the phospholipids lead to the delocalization of membrane bound proteins, thus contributing to the cell's destruction. The changes made to the membrane appeared to be not dependent on the composition of the phospholipid bilayer. Conclusions: The distortion caused to the fluidity of the membrane by the AMPs is sufficient to facilitate the entering of the peptides and leakage of the cytosol. General significance: Here we show in vivo that cationic AMPs cause “membrane leaks” at the site of membrane insertion by altering the organization and fluidity of the membrane. Our findings thus contribute to the understanding of the membrane perturbation characteristic of cationic AMPs.

AB - Background: Amphipathic cationic antimicrobial peptides (AMPs) TC19 and TC84, derived from the major AMPs of human blood platelets, thrombocidins, and Bactericidal Peptide 2 (BP2), a synthetic designer peptide showed to perturb the membrane of Bacillus subtilis. We aimed to determine the means by which the three AMPs cause membrane perturbation in vivo using B. subtilis and to evaluate whether the membrane alterations are dependent on the phospholipid composition of the membrane. Methods: Physiological analysis was employed using Alexa Fluor 488 labelled TC84, various fluorescence dyes, fluorescent microscopy techniques and structured illumination microscopy. Results: TC19, TC84 and BP2 created extensive fluidity domains in the membrane that are permeable, thus facilitating the entering of the peptides and the leakage of the cytosol. The direct interaction of the peptides with the bilayer create the fluid domains. The changes caused in the packing of the phospholipids lead to the delocalization of membrane bound proteins, thus contributing to the cell's destruction. The changes made to the membrane appeared to be not dependent on the composition of the phospholipid bilayer. Conclusions: The distortion caused to the fluidity of the membrane by the AMPs is sufficient to facilitate the entering of the peptides and leakage of the cytosol. General significance: Here we show in vivo that cationic AMPs cause “membrane leaks” at the site of membrane insertion by altering the organization and fluidity of the membrane. Our findings thus contribute to the understanding of the membrane perturbation characteristic of cationic AMPs.

UR - https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85048705264&origin=inward

UR - https://www.ncbi.nlm.nih.gov/pubmed/29902419

U2 - 10.1016/j.bbamem.2018.06.004

DO - 10.1016/j.bbamem.2018.06.004

M3 - Article

C2 - 29902419

VL - 1860

SP - 2404

EP - 2415

JO - BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

JF - BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

SN - 0005-2736

IS - 11

ER -

ID: 5529910