| LEBER, R., M. PACHLER, Ivo KABELKA, I. SVOBODA, D. KOLLER, Robert VÁCHA, K. LOHNER and G. PABST. Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain. Biophysical Journal. New York, USA: Cell Press, 2018, vol. 114, No 8, p. 1945-1954. ISSN 0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2018.03.006. |
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@article{1433963,
author = {Leber, R. and Pachler, M. and Kabelka, Ivo and Svoboda, I. and Koller, D. and Vácha, Robert and Lohner, K. and Pabst, G.},
article_location = {New York, USA},
article_number = {8},
doi = {http://dx.doi.org/10.1016/j.bpj.2018.03.006},
keywords = {MONOLAYER SPONTANEOUS CURVATURE; RAPID SOLVENT EXCHANGE; HOST-DEFENSE PEPTIDES; MAGAININ 2; ANTIBIOTIC PEPTIDE; ESCHERICHIA-COLI; ACTIVE PEPTIDES; PGLA; MECHANISM; BILAYERS},
language = {eng},
issn = {0006-3495},
journal = {Biophysical Journal},
title = {Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain.},
volume = {114},
year = {2018}
}
TY - JOUR
ID - 1433963
AU - Leber, R. - Pachler, M. - Kabelka, Ivo - Svoboda, I. - Koller, D. - Vácha, Robert - Lohner, K. - Pabst, G.
PY - 2018
TI - Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain.
JF - Biophysical Journal
VL - 114
IS - 8
SP - 1945-1954
EP - 1945-1954
PB - Cell Press
SN - 00063495
KW - MONOLAYER SPONTANEOUS CURVATURE
KW - RAPID SOLVENT EXCHANGE
KW - HOST-DEFENSE PEPTIDES
KW - MAGAININ 2
KW - ANTIBIOTIC PEPTIDE
KW - ESCHERICHIA-COLI
KW - ACTIVE PEPTIDES
KW - PGLA
KW - MECHANISM
KW - BILAYERS
N2 - Mixtures of the frog peptides magainin 2 and PGLa are well-known for their pronounced synergistic killing of Gram-negative bacteria. We aimed to gain insight into the underlying biophysical mechanism by interrogating the permeabilizing efficacies of the peptides as a function of stored membrane curvature strain. For Gram-negative bacterial-inner-membrane mimics, synergism was only observed when the anionic bilayers exhibited significant negative intrinsic curvatures imposed by monounsaturated phosphatidylethanolamine. In contrast, the peptides and their mixtures did not exhibit significant activities in charge-neutral mammalian mimics, including those with negative curvature, which is consistent with the requirement of charge-mediated peptide binding to the membrane. Our experimental findings are supported by computer simulations showing a significant decrease of the peptide-insertion free energy in membranes upon shifting intrinsic curvatures toward more positive values. The physiological relevance of our model studies is corroborated by a remarkable agreement with the peptide's synergistic activity in Escherichia coli. We propose that synergism is related to a lowering of a membrane-curvature-strain-mediated free-energy barrier by PGLa that assists membrane insertion of magainin 2, and not by strict pairwise interactions of the two peptides as suggested previously.
ER -
LEBER, R., M. PACHLER, Ivo KABELKA, I. SVOBODA, D. KOLLER, Robert VÁCHA, K. LOHNER and G. PABST. Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain. \textit{Biophysical Journal}. New York, USA: Cell Press, 2018, vol.~114, No~8, p.~1945-1954. ISSN~0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2018.03.006.
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