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

J 2020

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

IZADI, Nasim; Hana ČERNOCKÁ; Mojmír TREFULKA a Veronika OSTATNÁ

Základní údaje

Originální název

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

Autoři

IZADI, Nasim; Hana ČERNOCKÁ; Mojmír TREFULKA a Veronika OSTATNÁ

Vydání

ChemPlusChem, Weinheim, Wiley-VCH Verlag GmbH, 2020, 2192-6506

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.863

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/20:00116572

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

constant current chronopotentiometry; electrochemical analysis; glycoproteins; glycosylation; protein modifications

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 23. 10. 2020 12:30, Mgr. Marie Novosadová Šípková, DiS.

Anotace

V originále

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.

Citovat

IZADI, Nasim; Hana ČERNOCKÁ; Mojmír TREFULKA a Veronika OSTATNÁ. Influence of Protein Modification and Glycosylation in the Catalytic Hydrogen Evolution Reaction of Avidin and Neutravidin: An Electrochemical Analysis. ChemPlusChem. Weinheim: Wiley-VCH Verlag GmbH, 2020, roč. 85, č. 6, s. 1347-1353. ISSN 2192-6506. Dostupné z: https://doi.org/10.1002/cplu.202000298.

@article{1683136,
   author = {Izadi, Nasim and Černocká, Hana and Trefulka, Mojmír and Ostatná, Veronika},
   article_location = {Weinheim},
   article_number = {6},
   doi = {https://doi.org/10.1002/cplu.202000298},
   keywords = {constant current chronopotentiometry; electrochemical analysis; glycoproteins; glycosylation; protein modifications},
   language = {eng},
   issn = {2192-6506},
   journal = {ChemPlusChem},
   title = {Influence of Protein Modification and Glycosylation in the Catalytic Hydrogen Evolution Reaction of Avidin and Neutravidin: An Electrochemical Analysis},
   url = {https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/cplu.202000298},
   volume = {85},
   year = {2020}
}

TY  - JOUR
ID  - 1683136
AU  - Izadi, Nasim - Černocká, Hana - Trefulka, Mojmír - Ostatná, Veronika
PY  - 2020
TI  - Influence of Protein Modification and Glycosylation in the Catalytic Hydrogen Evolution Reaction of Avidin and Neutravidin: An Electrochemical Analysis
JF  - ChemPlusChem
VL  - 85
IS  - 6
SP  - 1347-1353
EP  - 1347-1353
PB  - Wiley-VCH Verlag GmbH
SN  - 21926506
KW  - constant current chronopotentiometry
KW  - electrochemical analysis
KW  - glycoproteins
KW  - glycosylation
KW  - protein modifications
UR  - https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/cplu.202000298
L2  - https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/cplu.202000298
N2  - 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.
ER  -

IZADI, Nasim; Hana ČERNOCKÁ; Mojmír TREFULKA a Veronika OSTATNÁ. Influence of Protein Modification and Glycosylation in the Catalytic Hydrogen Evolution Reaction of Avidin and Neutravidin: An Electrochemical Analysis. \textit{ChemPlusChem}. Weinheim: Wiley-VCH Verlag GmbH, 2020, roč.~85, č.~6, s.~1347-1353. ISSN~2192-6506. Dostupné z: https://doi.org/10.1002/cplu.202000298.

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