Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F18%3A00101149" target="_blank" >RIV/00216224:14740/18:00101149 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.bpj.2018.03.006" target="_blank" >http://dx.doi.org/10.1016/j.bpj.2018.03.006</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bpj.2018.03.006" target="_blank" >10.1016/j.bpj.2018.03.006</a>
Alternative languages
Result language
angličtina
Original language name
Synergism of Antimicrobial Frog Peptides Couples to Membrane Intrinsic Curvature Strain.
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biophysical Journal
ISSN
0006-3495
e-ISSN
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Volume of the periodical
114
Issue of the periodical within the volume
8
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
1945-1954
UT code for WoS article
000432692800018
EID of the result in the Scopus database
2-s2.0-85046539485