Electrogenic transport of Na+/K+-ATPase incorporated in lipidic cubic phases as a model biomimetic membrane

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F19%3A73596140" target="_blank" >RIV/61989592:15110/19:73596140 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0013468619307686?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0013468619307686?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2019.04.082" target="_blank" >10.1016/j.electacta.2019.04.082</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Electrogenic transport of Na+/K+-ATPase incorporated in lipidic cubic phases as a model biomimetic membrane

Popis výsledku v původním jazyce

The transmembrane pump Na + /K + -ATPase was reconstituted within a model membrane-mimetic system of monoolein liquid-crystalline cubic phase (LCP). LCP consists of a curved lipid bilayer forming the walls of a network of aqueous channels providing the lipid environment for the hydrophobic part of Na + /K + -ATPase, with the aqueous channels enabling protein contact with the aqueous environment. Electrogenic ion transport by Na + /K + -ATPase was investigated by chronoamperometry (CA). The results of the electrochemical measurements were compared with the spectroscopic assay of the protein activity. The transient currents were recorded following application of potential steps to the LCP modified electrode. Na + /K + -ATPase embedded in the lipidic part of the cubic phase transports cations across the mesophase film. Moreover, the lack of Na + halted protein function because Na + ions are required to promote the enzyme switching to P-E2 conformation. A specific Na + /K + -ATPase inhibitor, ouabain, added to the solution decreased ion transport abilities of the protein. Small-angle X-ray scattering (SAXS) measurements showed that the structure of cubic phase with incorporated Na + /K + -ATPase before and after the chronoamperometry experiments remained unchanged, and that the observed difference in current flowing through the cubic phase film with and without the protein was due to Na + /K + -ATPase activity in this environment.

Název v anglickém jazyce

Electrogenic transport of Na+/K+-ATPase incorporated in lipidic cubic phases as a model biomimetic membrane

Popis výsledku anglicky

The transmembrane pump Na + /K + -ATPase was reconstituted within a model membrane-mimetic system of monoolein liquid-crystalline cubic phase (LCP). LCP consists of a curved lipid bilayer forming the walls of a network of aqueous channels providing the lipid environment for the hydrophobic part of Na + /K + -ATPase, with the aqueous channels enabling protein contact with the aqueous environment. Electrogenic ion transport by Na + /K + -ATPase was investigated by chronoamperometry (CA). The results of the electrochemical measurements were compared with the spectroscopic assay of the protein activity. The transient currents were recorded following application of potential steps to the LCP modified electrode. Na + /K + -ATPase embedded in the lipidic part of the cubic phase transports cations across the mesophase film. Moreover, the lack of Na + halted protein function because Na + ions are required to promote the enzyme switching to P-E2 conformation. A specific Na + /K + -ATPase inhibitor, ouabain, added to the solution decreased ion transport abilities of the protein. Small-angle X-ray scattering (SAXS) measurements showed that the structure of cubic phase with incorporated Na + /K + -ATPase before and after the chronoamperometry experiments remained unchanged, and that the observed difference in current flowing through the cubic phase film with and without the protein was due to Na + /K + -ATPase activity in this environment.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

ELECTROCHIMICA ACTA

ISSN

0013-4686

e-ISSN

—

Svazek periodika

310

Číslo periodika v rámci svazku

July

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

113-121

Kód UT WoS článku

000467691200013

EID výsledku v databázi Scopus

2-s2.0-85064711290