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

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    SYSNO ASEP0525619
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleInfluence of Protein Modification and Glycosylation in the Catalytic Hydrogen Evolution Reaction of Avidin and Neutravidin: An Electrochemical Analysis
    Author(s) Izadi, Nasim (BFU-R) ORCID
    Černocká, Hana (BFU-R) RID, ORCID
    Trefulka, Mojmír (BFU-R) RID, ORCID
    Ostatná, Veronika (BFU-R) RID, ORCID
    Number of authors4
    Source TitleChemPlusChem. - : Wiley - ISSN 2192-6506
    Roč. 85, č. 6 (2020), s. 1347-1353
    Number of pages7 s.
    Publication formPrint - P
    Languageeng - English
    CountryDE - Germany
    Keywordsstreptavidin ; acid ; binding ; mercury ; signals
    Subject RIVCG - Electrochemistry
    OECD categoryElectrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)
    R&D ProjectsGA18-18154S GA ČR - Czech Science Foundation (CSF)
    Method of publishingLimited access
    Institutional supportBFU-R - RVO:68081707
    UT WOS000544057700029
    EID SCOPUS85086975479
    DOI10.1002/cplu.202000298
    AnnotationTo 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.
    WorkplaceInstitute of Biophysics
    ContactJana Poláková, polakova@ibp.cz, Tel.: 541 517 244
    Year of Publishing2021
    Electronic addresshttps://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/cplu.202000298
Number of the records: 1  

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