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.

Basic information

Original name

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

Authors

PACHLER, M., Ivo KABELKA (203 Czech Republic, belonging to the institution), R. LEBER, I. LETOFSKY-PAPST, K. LOHNER, Robert VÁCHA (203 Czech Republic, guarantor, belonging to the institution) and G. PABST

Edition

63rd Annual Meeting of the Biophysical-Society, 2019

Other information

Language

English

Type of outcome

Konferenční abstrakt

Field of Study

10403 Physical chemistry

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 3.854

RIV identification code

RIV/00216224:14740/19:00113469

Organization unit

Central European Institute of Technology

ISSN

DOI

http://dx.doi.org/10.1016/j.bpj.2018.11.280

UT WoS

000460779800219

Keywords in English

Magainin

Abstract

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 and 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. Available from: https://dx.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 = {http://dx.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 and 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. Available from: https://dx.doi.org/10.1016/j.bpj.2018.11.280.

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