Determining the Functional Oligomeric State of Membrane- Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F23%3A00572771" target="_blank" >RIV/61388955:_____/23:00572771 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11320/23:10464122

Výsledek na webu

<a href="https://hdl.handle.net/11104/0343342" target="_blank" >https://hdl.handle.net/11104/0343342</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.analchem.2c05692" target="_blank" >10.1021/acs.analchem.2c05692</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Determining the Functional Oligomeric State of Membrane- Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles

Popis výsledku v původním jazyce

Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to their physiological functions. This phenomenon makes it difficult to identify the functional oligomeric states of membrane lipid interacting proteins, for example, during the formation of transient membrane pores. Using fibroblast growth factor 2 (FGF2) as an example, we present a methodology applicable to giant lipid vesicles by which functional oligomers can be distinguished from nonspecifically aggregated proteins without functionality. Two distinct populations of fibroblast growth factor 2 were identified with (i) dimers to hexamers and (ii) a broad population of higher oligomeric states of membrane associated FGF2 oligomers significantly distorting the original unfiltered histogram of all detectable oligomeric species of FGF2. The presented statistical approach is relevant for various techniques for characterizing membrane-dependent protein oligomerization.

Název v anglickém jazyce

Determining the Functional Oligomeric State of Membrane- Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles

Popis výsledku anglicky

Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to their physiological functions. This phenomenon makes it difficult to identify the functional oligomeric states of membrane lipid interacting proteins, for example, during the formation of transient membrane pores. Using fibroblast growth factor 2 (FGF2) as an example, we present a methodology applicable to giant lipid vesicles by which functional oligomers can be distinguished from nonspecifically aggregated proteins without functionality. Two distinct populations of fibroblast growth factor 2 were identified with (i) dimers to hexamers and (ii) a broad population of higher oligomeric states of membrane associated FGF2 oligomers significantly distorting the original unfiltered histogram of all detectable oligomeric species of FGF2. The presented statistical approach is relevant for various techniques for characterizing membrane-dependent protein oligomerization.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

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

Rok uplatnění

2023

Kód důvěrnosti údajů

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

Název periodika

Analytical Chemistry

ISSN

0003-2700

e-ISSN

1520-6882

Svazek periodika

95

Číslo periodika v rámci svazku

23

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

8807-8815

Kód UT WoS článku

000985563200001

EID výsledku v databázi Scopus

2-s2.0-85159619887