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 and Ondrej ŠEDO

Basic information

Original name

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

Authors

OSTATNÁ, Veronika (703 Slovakia), V. KASALOVA (203 Czech Republic), K. KMETOVA (203 Czech Republic) and Ondrej ŠEDO (203 Czech Republic, guarantor, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10406 Analytical chemistry

Country of publisher

Switzerland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 3.218

RIV identification code

RIV/00216224:14740/18:00106758

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000437818600016

Keywords in English

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

Abstract

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.

Links

LM2015043, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

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

Detailed Information on Publication Record