Optimal conditions for opening of membrane pore by amphiphilic peptides
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00081581" target="_blank" >RIV/00216224:14740/15:00081581 - isvavai.cz</a>
Result on the web
<a href="http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229" target="_blank" >http://scitation.aip.org/content/aip/journal/jcp/143/24/10.1063/1.4933229</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1063/1.4933229" target="_blank" >10.1063/1.4933229</a>
Alternative languages
Result language
angličtina
Original language name
Optimal conditions for opening of membrane pore by amphiphilic peptides
Original language description
Amphiphilic peptides can interact with biological membranes and severely affect their barrier and signaling functions. These peptides, including antimicrobial peptides, can self-assemble into transmembrane pores that cause cell death. Despite their medical importance, the conditions required for pore formation remain elusive. Monte Carlo simulations with coarse-grained models enabled us to calculate the free energies of pore opening under various conditions. In agreement with oriented circular dichroismexperiments, a high peptide-to-lipid ratio was found to be necessary for spontaneous pore assembly. The peptide length has a non-monotonic impact on pore formation, and the optimal length matches with the membrane thickness. Furthermore, the hydrophobicity of the peptide ends and the mutual positions of peptides on the membrane play a role.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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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
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
JOURNAL OF CHEMICAL PHYSICS
ISSN
0021-9606
e-ISSN
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Volume of the periodical
143
Issue of the periodical within the volume
24
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
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UT code for WoS article
000370412900021
EID of the result in the Scopus database
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