Interleaflet organization of membrane nanodomains: What can(not) be resolved by FRET?
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F23%3A00572784" target="_blank" >RIV/61388955:_____/23:00572784 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00216208:11310/23:10451120 RIV/00216208:11320/23:10451120
Výsledek na webu
<a href="https://hdl.handle.net/11104/0343351" target="_blank" >https://hdl.handle.net/11104/0343351</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bpj.2022.11.014" target="_blank" >10.1016/j.bpj.2022.11.014</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Interleaflet organization of membrane nanodomains: What can(not) be resolved by FRET?
Popis výsledku v původním jazyce
Plasma membranes as well as their simplified model systems show an inherent nanoscale heterogeneity. As a result of strong interleaflet interactions, these nanoheterogeneities (called here lipid nanodomains) can be found in perfect registration (i.e., nanodomains in the inner leaflet are registered with the nanodomains in the outer leaflet). Alternatively, they might be interleaflet independent, antiregistered, or located asymmetrically in one bilayer leaflet only. To distinguish these scenarios from each other appears to be an experimental challenge. In this work, we analyzed the potential of Förster resonance energy transfer to characterize interleaflet organization of nanodomains. We generated in silico time-resolved fluorescence decays for a large set of virtual as well as real donor/acceptor pairs distributed over the bilayer containing registered, independent, antiregistered, or asymmetrically distributed nanodomains. In this way, we were able to identify conditions that gave satisfactory or unsatisfactory resolution. Overall, Förster resonance energy transfer appears as a robust method that, when using donor/acceptor pairs with good characteristics, yields otherwise difficult-to-reach characteristics of membrane lipid nanodomains.
Název v anglickém jazyce
Interleaflet organization of membrane nanodomains: What can(not) be resolved by FRET?
Popis výsledku anglicky
Plasma membranes as well as their simplified model systems show an inherent nanoscale heterogeneity. As a result of strong interleaflet interactions, these nanoheterogeneities (called here lipid nanodomains) can be found in perfect registration (i.e., nanodomains in the inner leaflet are registered with the nanodomains in the outer leaflet). Alternatively, they might be interleaflet independent, antiregistered, or located asymmetrically in one bilayer leaflet only. To distinguish these scenarios from each other appears to be an experimental challenge. In this work, we analyzed the potential of Förster resonance energy transfer to characterize interleaflet organization of nanodomains. We generated in silico time-resolved fluorescence decays for a large set of virtual as well as real donor/acceptor pairs distributed over the bilayer containing registered, independent, antiregistered, or asymmetrically distributed nanodomains. In this way, we were able to identify conditions that gave satisfactory or unsatisfactory resolution. Overall, Förster resonance energy transfer appears as a robust method that, when using donor/acceptor pairs with good characteristics, yields otherwise difficult-to-reach characteristics of membrane lipid nanodomains.
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
<a href="/cs/project/GC20-01401J" target="_blank" >GC20-01401J: Studium vztahu struktury a funkce FGF2 oligomerů tvořících membránové póry technikami zaměřenými na sledování jedné molekuly</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2023
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Biophysical Journal
ISSN
0006-3495
e-ISSN
1542-0086
Svazek periodika
122
Číslo periodika v rámci svazku
11
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
15
Strana od-do
2053-2067
Kód UT WoS článku
001053565300001
EID výsledku v databázi Scopus
2-s2.0-85142851949