Distinct roles of SNARE-mimicking lipopeptides during initial steps of membrane fusion
Identifikátory výsledku
Kód výsledku v 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>
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Distinct roles of SNARE-mimicking lipopeptides during initial steps of membrane fusion
Popis výsledku v původním jazyce
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
Název v anglickém jazyce
Distinct roles of SNARE-mimicking lipopeptides during initial steps of membrane fusion
Popis výsledku anglicky
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
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10403 - Physical chemistry
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2018
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Nanoscale
ISSN
2040-3364
e-ISSN
—
Svazek periodika
10
Číslo periodika v rámci svazku
40
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
10
Strana od-do
19064-19073
Kód UT WoS článku
000448344100020
EID výsledku v databázi Scopus
2-s2.0-85055080629