Influence of Protein Modification and Glycosylation in the Catalytic Hydrogen Evolution Reaction of Avidin and Neutravidin: An Electrochemical Analysis

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F20%3A00525619" target="_blank" >RIV/68081707:_____/20:00525619 - isvavai.cz</a>
Alternative codes found
RIV/00216224:14310/20:00116572
Result on the web
<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/cplu.202000298" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/cplu.202000298</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/cplu.202000298" target="_blank" >10.1002/cplu.202000298</a>

Result language
angličtina
Original language name
Influence of Protein Modification and Glycosylation in the Catalytic Hydrogen Evolution Reaction of Avidin and Neutravidin: An Electrochemical Analysis
Original language description
To investigate glycans' influence on the behavior of glycoproteins on charged surfaces, avidin and its nonglycosylated and neutralized version neutravidin were studied by label-free chronopotentiometric stripping (CPS) analysis and alternating current voltammetry combined with a mercury electrode. Despite neutravidin's and avidin's similar size and structure, their CPS responses differed due to the different amounts of catalytically active free amino groups of lysine and arginine residues. Acetylation of the proteins resulted in the suppression of their CPS responses by almost four times for avidin and by about 50 % for neutravidin, respectively. On the other hand, the presence of glycans in the acetylated avidin induced about 30 % higher chronopotentiometric response compared to the acetylated neutravidin. We suggest that the presence, size and composition of the glycans influenced the CPS signal due to differences in the orientation at a charged surface. The obtained results can be utilized in glycoprotein research.
Czech name
—
Czech description
—

Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Project
<a href="/en/project/GA18-18154S" target="_blank" >GA18-18154S: New tools of label-free electrochemical analysis of protein interactions with nucleic acids and proteins</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)