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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 ASEP 0525619 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Influence 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, ORCIDNumber of authors 4 Source Title ChemPlusChem. - : Wiley - ISSN 2192-6506
Roč. 85, č. 6 (2020), s. 1347-1353Number of pages 7 s. Publication form Print - P Language eng - English Country DE - Germany Keywords streptavidin ; acid ; binding ; mercury ; signals Subject RIV CG - Electrochemistry OECD category Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis) R&D Projects GA18-18154S GA ČR - Czech Science Foundation (CSF) Method of publishing Limited access Institutional support BFU-R - RVO:68081707 UT WOS 000544057700029 EID SCOPUS 85086975479 DOI 10.1002/cplu.202000298 Annotation 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. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2021 Electronic address https://chemistry-europe.onlinelibrary.wiley.com/doi/full/10.1002/cplu.202000298
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