Synergism of Magainins is Not Coupled to the Formation of a
Well-Defined Peptide Pore

a 2019

Synergism of Magainins is Not Coupled to the Formation of a Well-Defined Peptide Pore

PACHLER, M.; Ivo KABELKA; R. LEBER; I. LETOFSKY-PAPST; K. LOHNER et al.

Základní údaje

Originální název

Synergism of Magainins is Not Coupled to the Formation of a Well-Defined Peptide Pore

Autoři

PACHLER, M.; Ivo KABELKA ; R. LEBER; I. LETOFSKY-PAPST; K. LOHNER; Robert VÁCHA a G. PABST

Vydání

63rd Annual Meeting of the Biophysical-Society, 2019

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10403 Physical chemistry

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 3.854

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/19:00113469

Organizační jednotka

Středoevropský technologický institut

ISSN

DOI

https://doi.org/10.1016/j.bpj.2018.11.280

UT WoS

000460779800219

Klíčová slova anglicky

Magainin

Štítky

rivok

Příznaky

Mezinárodní význam

Změněno: 1. 4. 2020 15:57, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

We have studied the synergistic activity of PGLa and MG2a, two antimicrobial peptides secreted by the African clawed frog, on phosphatidylethanolamine/phosphatidylglycerol mimics of the inner membrane of Gram negative bacteria using an array of experimental and theoretical techniques. In particular, we correlated the peptides’ dye-releasing capabilities from large unilamellar vesicles with the induced structural changes on the microscopic to nanoscopic length scales combining small-angle X-ray and neutron scattering with transmission electron microscopy and molecular dynamics simulations. At low concentrations and in the absence of pronounced dye leakage we found that MG2a is aligned parallel to the membrane surface in the lipid’s headgroup region and causes a relocation of PGLa from the backbone region toward the polar surface. In the synergistic regime, i.e. at high concentrations, the peptides transformed the unilamellar vesicles into collapsed multilamellar liposomes with the peptides acting as spacers between the bilayers. In this case, the PGLa and MG2a do not exhibit strong cross-interactions and show the tendency to form fiber-like structures. PGLa and MG2a synergism in phosphatidylethanolamine/phosphatidylglycerol mixtures consequently does not involve the formation of a stable peptide pore within the bilayer as conceived previously.

Citovat

PACHLER, M.; Ivo KABELKA; R. LEBER; I. LETOFSKY-PAPST; K. LOHNER; Robert VÁCHA a G. PABST. Synergism of Magainins is Not Coupled to the Formation of a Well-Defined Peptide Pore. In 63rd Annual Meeting of the Biophysical-Society. 2019. ISSN 0006-3495. Dostupné z: https://doi.org/10.1016/j.bpj.2018.11.280.

@proceedings{1641750,
   author = {Pachler, M. and Kabelka, Ivo and Leber, R. and LetofskyandPapst, I. and Lohner, K. and Vácha, Robert and Pabst, G.},
   booktitle = {63rd Annual Meeting of the Biophysical-Society},
   doi = {https://doi.org/10.1016/j.bpj.2018.11.280},
   keywords = {Magainin},
   language = {eng},
   title = {Synergism of Magainins is Not Coupled to the Formation of a Well-Defined Peptide Pore},
   year = {2019}
}

TY  - CONF
ID  - 1641750
AU  - Pachler, M. - Kabelka, Ivo - Leber, R. - Letofsky-Papst, I. - Lohner, K. - Vácha, Robert - Pabst, G.
PY  - 2019
TI  - Synergism of Magainins is Not Coupled to the Formation of a Well-Defined Peptide Pore
KW  - Magainin
N2  - We have studied the synergistic activity of PGLa and MG2a, two antimicrobial peptides secreted by the African clawed frog, on phosphatidylethanolamine/phosphatidylglycerol mimics of the inner membrane of Gram negative bacteria using an array of experimental and theoretical techniques. In particular, we correlated the peptides’ dye-releasing capabilities from large unilamellar vesicles with the induced structural changes on the microscopic to nanoscopic length scales combining small-angle X-ray and neutron scattering with transmission electron microscopy and molecular dynamics simulations. At low concentrations and in the absence of pronounced dye leakage we found that MG2a is aligned parallel to the membrane surface in the lipid’s headgroup region and causes a relocation of PGLa from the backbone region toward the polar surface. In the synergistic regime, i.e. at high concentrations, the peptides transformed the unilamellar vesicles into collapsed multilamellar liposomes with the peptides acting as spacers between the bilayers. In this case, the PGLa and MG2a do not exhibit strong cross-interactions and show the tendency to form fiber-like structures. PGLa and MG2a synergism in phosphatidylethanolamine/phosphatidylglycerol mixtures consequently does not involve the formation of a stable peptide pore within the bilayer as conceived previously.
ER  -

PACHLER, M.; Ivo KABELKA; R. LEBER; I. LETOFSKY-PAPST; K. LOHNER; Robert VÁCHA a G. PABST. Synergism of Magainins is Not Coupled to the Formation of a Well-Defined Peptide Pore. In \textit{63rd Annual Meeting of the Biophysical-Society}. 2019. ISSN~0006-3495. Dostupné z: https://doi.org/10.1016/j.bpj.2018.11.280.

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