Controlled Peptide-Mediated Vesicle Fusion Assessed by Simultaneous Dual-Colour Time-Lapsed Fluorescence Microscopy

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F20%3A00522602" target="_blank" >RIV/61388955:_____/20:00522602 - isvavai.cz</a>

Výsledek na webu

<a href="http://hdl.handle.net/11104/0307069" target="_blank" >http://hdl.handle.net/11104/0307069</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41598-020-59926-z" target="_blank" >10.1038/s41598-020-59926-z</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Controlled Peptide-Mediated Vesicle Fusion Assessed by Simultaneous Dual-Colour Time-Lapsed Fluorescence Microscopy

Popis výsledku v původním jazyce

We have employed a model system, inspired by SnARe proteins, to facilitate membrane fusion between Giant Unilamellar Vesicles (GUVs) and Large Unilamellar Vesicles (LUVs) under physiological conditions. in this system, two synthetic lipopeptide constructs comprising the coiled-coil heterodimer-forming peptides K4, (KiAALKe)4, or e4, (eiAALeK)4, a peG spacer of variable length, and a cholesterol moiety to anchor the peptides into the liposome membrane replace the natural SnARe proteins. GUVs are functionalized with one of the lipopeptide constructs and the fusion process is triggered by adding LUVs bearing the complementary lipopeptide. Dual-colour time lapse fluorescence microscopy was used to visualize lipid- and content-mixing. Using conventional confocal microscopy, lipid mixing was observed on the lipid bilayer of individual GUVs. in addition to lipid-mixing, content-mixing assays showed a low efficiency due to clustering of K4-functionalized LUVs on the GUVs target membranes. We showed that, through the use of the non-ionic surfactant Tween 20, content-mixing between GUVs and LUVs could be improved, meaning this system has the potential to be employed for drug delivery in biological systems.

Název v anglickém jazyce

Controlled Peptide-Mediated Vesicle Fusion Assessed by Simultaneous Dual-Colour Time-Lapsed Fluorescence Microscopy

Popis výsledku anglicky

We have employed a model system, inspired by SnARe proteins, to facilitate membrane fusion between Giant Unilamellar Vesicles (GUVs) and Large Unilamellar Vesicles (LUVs) under physiological conditions. in this system, two synthetic lipopeptide constructs comprising the coiled-coil heterodimer-forming peptides K4, (KiAALKe)4, or e4, (eiAALeK)4, a peG spacer of variable length, and a cholesterol moiety to anchor the peptides into the liposome membrane replace the natural SnARe proteins. GUVs are functionalized with one of the lipopeptide constructs and the fusion process is triggered by adding LUVs bearing the complementary lipopeptide. Dual-colour time lapse fluorescence microscopy was used to visualize lipid- and content-mixing. Using conventional confocal microscopy, lipid mixing was observed on the lipid bilayer of individual GUVs. in addition to lipid-mixing, content-mixing assays showed a low efficiency due to clustering of K4-functionalized LUVs on the GUVs target membranes. We showed that, through the use of the non-ionic surfactant Tween 20, content-mixing between GUVs and LUVs could be improved, meaning this system has the potential to be employed for drug delivery in biological systems.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Scientific Reports

ISSN

2045-2322

e-ISSN

—

Svazek periodika

10

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

3087

Kód UT WoS článku

000549177700001

EID výsledku v databázi Scopus

2-s2.0-85079777213