Lipidic liquid crystalline cubic phases for preparation of ATP-hydrolysing enzyme electrodes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F18%3A73588056" target="_blank" >RIV/61989592:15110/18:73588056 - isvavai.cz</a>
Result on the web
<a href="https://reader.elsevier.com/reader/sd/pii/S0956566317306449?token=4903F9D979210BF10F1A14679CA02C9979545227A39CEAAE679C79BBDA4321B37BCF542B6C300019FF6DF7D985AC5F2A" target="_blank" >https://reader.elsevier.com/reader/sd/pii/S0956566317306449?token=4903F9D979210BF10F1A14679CA02C9979545227A39CEAAE679C79BBDA4321B37BCF542B6C300019FF6DF7D985AC5F2A</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bios.2017.09.036" target="_blank" >10.1016/j.bios.2017.09.036</a>
Alternative languages
Result language
angličtina
Original language name
Lipidic liquid crystalline cubic phases for preparation of ATP-hydrolysing enzyme electrodes
Original language description
he lipidic liquid-crystalline cubic phase (LCP) is a membrane-mimetic material useful for the stabilization and structural analysis of membrane proteins. Here, we focused on the incorporation of the membrane ATP-hydrolysing sodium/potassium transporter Na+/K+-ATPase (NKA) into a monoolein-derived LCP. Small-angle X-ray scattering was employed for the determination of the LCP structure, which was of Pn3m symmetry for all the formulations studied. The fully characterized NKA-LCP material was immobilized onto a glassy carbon electrode, forming a highly stable enzyme electrode and a novel sensing platform. A typical NKA voltammetric signature was monitored via the anodic reaction of tyrosine and tryptophan residues. The in situ enzyme activity evaluation was based on the ability of NKA to transform ATP to ADP and free phosphate, the latter reacting with ammonium molybdate to form the ammonium phosphomolybdate complex under acidic conditions. The square-wave voltammetric detection of phosphomolybdate was performed and complemented with spectrophotometric measurement at 710nm. The anodic voltammetric response, corresponding to the catalytic ATP-hydrolysing function of NKA incorporated into the LCP, was monitored at around + 0.2V vs. Ag/AgCl in the presence or absence of ouabain, a specific NKA inhibitor. NKA incorporated into the LCP retained its ATP-hydrolysing activity for 7 days, while the solubilized protein became practically inactive. The novelty of this work is the first incorporation of NKA into a lipidic cubic phase with consequent enzyme functionality and stability evaluation using voltammetric detection. The application of LCPs could also be important in the further development of new membrane protein electrochemical sensors and enzyme electrodes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - 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)
Result continuities
Project
<a href="/en/project/GA14-08032S" target="_blank" >GA14-08032S: New approaches to the study of the intrinsic electroactivity of membrane proteins: focus on structural changes and molecular interactions</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
BIOSENSORS & BIOELECTRONICS
ISSN
0956-5663
e-ISSN
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Volume of the periodical
100
Issue of the periodical within the volume
February
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
8
Pages from-to
437-444
UT code for WoS article
000416187600055
EID of the result in the Scopus database
2-s2.0-85029913162