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

Result code in 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>

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

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

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2019

Confidentiality

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

Name of the periodical

ELECTROCHIMICA ACTA

ISSN

0013-4686

e-ISSN

—

Volume of the periodical

310

Issue of the periodical within the volume

July

Country of publishing house

GB - UNITED KINGDOM

Number of pages

9

Pages from-to

113-121

UT code for WoS article

000467691200013

EID of the result in the Scopus database

2-s2.0-85064711290