Other formats:
BibTeX
LaTeX
RIS
@article{1597058,
author = {Pachler, Michael and Kabelka, Ivo and Appavou, MarieandSousai and Lohner, Karl and Vácha, Robert and Pabst, Georg},
article_location = {New York},
article_number = {10},
doi = {http://dx.doi.org/10.1016/j.bpj.2019.10.022},
keywords = {X-RAY-SCATTERING; ANTIMICROBIAL PEPTIDES; FORCE-FIELD; DYNAMICS; BILAYERS; MODEL; SIMULATIONS; VALIDATION; POTENTIALS; DERIVATION},
language = {eng},
issn = {0006-3495},
journal = {Biophysical Journal},
title = {Magainin 2 and PGLa in Bacterial Membrane Mimics I: Peptide-Peptide and Lipid-Peptide Interactions.},
url = {https://www.sciencedirect.com/science/article/pii/S0006349519308707},
volume = {117},
year = {2019}
}
TY - JOUR
ID - 1597058
AU - Pachler, Michael - Kabelka, Ivo - Appavou, Marie-Sousai - Lohner, Karl - Vácha, Robert - Pabst, Georg
PY - 2019
TI - Magainin 2 and PGLa in Bacterial Membrane Mimics I: Peptide-Peptide and Lipid-Peptide Interactions.
JF - Biophysical Journal
VL - 117
IS - 10
SP - 1858-1869
EP - 1858-1869
PB - Cell Press
SN - 00063495
KW - X-RAY-SCATTERING
KW - ANTIMICROBIAL PEPTIDES
KW - FORCE-FIELD
KW - DYNAMICS
KW - BILAYERS
KW - MODEL
KW - SIMULATIONS
KW - VALIDATION
KW - POTENTIALS
KW - DERIVATION
UR - https://www.sciencedirect.com/science/article/pii/S0006349519308707
L2 - https://www.sciencedirect.com/science/article/pii/S0006349519308707
N2 - We addressed the onset of synergistic activity of the two well-studied antimicrobial peptides magainin 2 (MG2a) and PGLa using lipid-only mimics of Gram-negative cytoplasmic membranes. Specifically, we coupled a joint analysis of small-angle x-ray and neutron scattering experiments on fully hydrated lipid vesicles in the presence of MG2a and L18W-PGLa to all-atom and coarse-grained molecular dynamics simulations. In agreement with previous studies, both peptides, as well as their equimolar mixture, were found to remain upon adsorption in a surface-aligned topology and to induce significant membrane perturbation, as evidenced by membrane thinning and hydrocarbon order parameter changes in the vicinity of the inserted peptide. These effects were particularly pronounced for the so-called synergistic mixture of 1:1 (mol/mol) L18W-PGLa/MG2a and cannot be accounted for by a linear combination of the membrane perturbations of two peptides individually. Our data are consistent with the formation of parallel heterodimers at concentrations below a synergistic increase of dye leakage from vesicles. Our simulations further show that the heterodimers interact via salt bridges and hydrophobic forces, which apparently makes them more stable than putatively formed antiparallel L18W-PGLa and MG2a homodimers. Moreover, dimerization of L18W-PGLa and MG2a leads to a relocation of the peptides within the lipid headgroup region as compared to the individual peptides. The early onset of dimerization of L18W-PGLa and MG2a at low peptide concentrations consequently appears to be key to their synergistic dye-releasing activity from lipid vesicles at high concentrations.
ER -
PACHLER, Michael, Ivo KABELKA, Marie-Sousai APPAVOU, Karl LOHNER, Robert VÁCHA and Georg PABST. Magainin 2 and PGLa in Bacterial Membrane Mimics I: Peptide-Peptide and Lipid-Peptide Interactions. \textit{Biophysical Journal}. New York: Cell Press, 2019, vol.~117, No~10, p.~1858-1869. ISSN~0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2019.10.022.
|
