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Distinct roles of SNARE-mimicking lipopeptides during initial steps of membrane fusion

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F18%3A00495130" target="_blank" >RIV/61388955:_____/18:00495130 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1039/C8NR05730C" target="_blank" >http://dx.doi.org/10.1039/C8NR05730C</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/C8NR05730C" target="_blank" >10.1039/C8NR05730C</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Distinct roles of SNARE-mimicking lipopeptides during initial steps of membrane fusion

  • Original language description

    A model system for membrane fusion, inspired by SNARE proteins and based on two complementary lipopeptides CPnE4 and CPnK4, has been recently developed. It consists of cholesterol (C), a poly(ethylene glycol) linker (Pn) and either a cationic peptide K4 (KIAALKE)4 or an anionic peptide E4 (EIAALEK)4. In this paper, fluorescence spectroscopy is used to decipher distinct but complementary roles of these lipopeptides during early stages of membrane fusion. Molecular evidence is provided that different distances of E4 in CPnE4 and K4 in CPnK4 from the bilayer represent an important mechanism, which enables fusion. Whereas E4 is exposed to the bulk and solely promotes membrane binding of CPnK4, K4 loops back to the lipid–water interface where it fulfills two distinct roles: it initiates bilayer contact by binding to CPnE4 containing bilayers, and it initiates fusion by modulating the bilayer properties. The interaction between CPnE4 and CPnK4 is severely down-regulated by binding of K4 to the bilayer and possible only if the lipopeptides approach each other as constituents of different bilayers. When the complementary lipopeptides are localized in the same bilayer, hetero-coiling is disabled. These data provide crucial insights as to how fusion is initiated and highlight the importance of both peptides in this process.n

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

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

    Nanoscale

  • ISSN

    2040-3364

  • e-ISSN

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    40

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    10

  • Pages from-to

    19064-19073

  • UT code for WoS article

    000448344100020

  • EID of the result in the Scopus database

    2-s2.0-85055080629