Chronopotentiometric sensing of anterior gradient 2 protein

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F17%3A00077854" target="_blank" >RIV/00209805:_____/17:00077854 - isvavai.cz</a>

Alternative codes found

RIV/68081707:_____/17:00476126

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0013468617308320" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0013468617308320</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2017.04.090" target="_blank" >10.1016/j.electacta.2017.04.090</a>

Result language

angličtina

Original language name

Chronopotentiometric sensing of anterior gradient 2 protein

Original language description

The study of new proteins and particularly those involved in cancer development is still a focal point of interest. We studied the anterior gradient 2 (AGR2) oncoprotein, aberrantly expressed in a number of human cancers. For the first time the electrochemical behaviour of various variants of the AGR2 was described using constant current chronopotentiometric stripping (CPS) analysis at mercury electrodes. In the first part, we show that mutation of AGR2 protein at its sole cysteine significantly changed its CPS response compared to wild type AGR2, probably due to their different adsorption and some deviations in their structures, which were obtained by analysis of hydrogen deuterium (H/D) exchange connected with high resolution mass spectrometry (MS). In the second part we studied the influence of His-tag modification, widely used in the purification of recombinant proteins, on CPS response and H/D exchange. Addition of a His-tag, containing positively charged and electroactive residues, affected the CPS peak H of His6-tagged AGR2 compared to non-tagged AGR2 protein due to different adsorption as well as variation in the structure at the negatively charged interface. H/D exchange MS analysis confirmed differences in the structure of these two variants even in solution. The uncovering of AGR2 behaviour at charged surfaces gives us the opportunity to study its interactions with other biomedically important proteins.

Czech name

—

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

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

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

240

Issue of the periodical within the volume

20.6.2017

Country of publishing house

GB - UNITED KINGDOM

Number of pages

8

Pages from-to

250-257

UT code for WoS article

000402444800029

EID of the result in the Scopus database

2-s2.0-85018501696