Changes of electrocatalytic response of bovine serum albumin
after its methylation and acetylation

J 2018

Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation

OSTATNÁ, Veronika, V. KASALOVA, K. KMETOVA a Ondrej ŠEDO

Základní údaje

Originální název

Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation

Autoři

OSTATNÁ, Veronika (703 Slovensko), V. KASALOVA (203 Česká republika), K. KMETOVA (203 Česká republika) a Ondrej ŠEDO (203 Česká republika, garant, domácí)

Vydání

Journal of Electroanalytical Chemistry, Lausanne, Elsevier, 2018, 1572-6657

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10406 Analytical chemistry

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 3.218

Kód RIV

RIV/00216224:14740/18:00106758

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.jelechem.2017.11.044

UT WoS

000437818600016

Klíčová slova anglicky

Bovine serum albumin; Protein acetylation; Protein methylation; Electroactive residues; Catalytic hydrogen evolution reaction; Mercury electrode

Štítky

CF PROT, rivok

Změněno: 4. 4. 2019 19:19, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Post-translational modifications play the crucial role in biological systems and the identification of novel post translational modifications and study of their role are gaining much attention in proteomics research. For the first time, we compared methylated and acetylated bovine serum albumin to its native and denatured form using constant current chronopotentiometric stripping analysis, phase sensitive alternating current voltammetry and matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS). Our results showed that acetylation of bovine serum albumin resulted in decrease of chronopotentiometric peak H due to modification of electroactive residues, while predominantly non-electroactive residues were modified by methylation of serum albumin. Nevertheless, both modifications altered adsorption of protein at surface and therein influenced chronopotentiometric peak H. MALDI-TOF MS analysis confirmed modifications of serum albumin and was in good agreement with electrochemical results. The present results show the capability of label- and reagent-free electrochemical methods to detect post-translational modifications in proteins.

Návaznosti

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

Citovat

OSTATNÁ, Veronika, V. KASALOVA, K. KMETOVA a Ondrej ŠEDO. Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation. Journal of Electroanalytical Chemistry. Lausanne: Elsevier, 2018, roč. 821, JUL, s. 97-103. ISSN 1572-6657. Dostupné z: https://dx.doi.org/10.1016/j.jelechem.2017.11.044.

@article{1515977,
   author = {Ostatná, Veronika and Kasalova, V. and Kmetova, K. and Šedo, Ondrej},
   article_location = {Lausanne},
   article_number = {JUL},
   doi = {http://dx.doi.org/10.1016/j.jelechem.2017.11.044},
   keywords = {Bovine serum albumin; Protein acetylation; Protein methylation; Electroactive residues; Catalytic hydrogen evolution reaction; Mercury electrode},
   language = {eng},
   issn = {1572-6657},
   journal = {Journal of Electroanalytical Chemistry},
   title = {Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation},
   volume = {821},
   year = {2018}
}

TY  - JOUR
ID  - 1515977
AU  - Ostatná, Veronika - Kasalova, V. - Kmetova, K. - Šedo, Ondrej
PY  - 2018
TI  - Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation
JF  - Journal of Electroanalytical Chemistry
VL  - 821
IS  - JUL
SP  - 97-103
EP  - 97-103
PB  - Elsevier
SN  - 15726657
KW  - Bovine serum albumin
KW  - Protein acetylation
KW  - Protein methylation
KW  - Electroactive residues
KW  - Catalytic hydrogen evolution reaction
KW  - Mercury electrode
N2  - Post-translational modifications play the crucial role in biological systems and the identification of novel post translational modifications and study of their role are gaining much attention in proteomics research. For the first time, we compared methylated and acetylated bovine serum albumin to its native and denatured form using constant current chronopotentiometric stripping analysis, phase sensitive alternating current voltammetry and matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS). Our results showed that acetylation of bovine serum albumin resulted in decrease of chronopotentiometric peak H due to modification of electroactive residues, while predominantly non-electroactive residues were modified by methylation of serum albumin. Nevertheless, both modifications altered adsorption of protein at surface and therein influenced chronopotentiometric peak H. MALDI-TOF MS analysis confirmed modifications of serum albumin and was in good agreement with electrochemical results. The present results show the capability of label- and reagent-free electrochemical methods to detect post-translational modifications in proteins.
ER  -

OSTATNÁ, Veronika, V. KASALOVA, K. KMETOVA a Ondrej ŠEDO. Changes of electrocatalytic response of bovine serum albumin after its methylation and acetylation. \textit{Journal of Electroanalytical Chemistry}. Lausanne: Elsevier, 2018, roč.~821, JUL, s.~97-103. ISSN~1572-6657. Dostupné z: https://dx.doi.org/10.1016/j.jelechem.2017.11.044.

Podrobný výpis o publikaci