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Modification of a Mercury Electrode with Different Thioalkanes: Structure-Sensitive Bovine Serum Albumin Analysis

SYSNO ASEP	0491232
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Modification of a Mercury Electrode with Different Thioalkanes: Structure-Sensitive Bovine Serum Albumin Analysis
Author(s)	Ostatná, Veronika (BFU-R)_{RID, ORCID} Černocká, Hana (BFU-R)_{RID, ORCID} Hasoň, Stanislav (BFU-R)_{RID, ORCID} Paleček, Emil (BFU-R)_{RID, ORCID}
Number of authors	4
Source Title	ChemElectroChem. - : Wiley - ISSN 2196-0216 Roč. 5, č. 10 (2018), s. 1373-1379
Number of pages	7 s.
Publication form	Print - P
Language	eng - English
Country	DE - Germany
Keywords	self-assembled monolayers ; electroanalytical chemistry ; electrochemical detection ; amalgam electrodes
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)
Institutional support	BFU-R - RVO:68081707
UT WOS	000431974500006
DOI	10.1002/celc.201800275
Annotation	Chronopotentiometric stripping (CPS) in combination with mercury electrodes is convenient for structure-sensitive protein analysis. By using this method, we tested the discrimination between native and denatured bovine serum albumin (BSA) at various alkanethiol self-assembled monolayers (SAMs). Our results showed that alkanethiol SAMs with different headgroups or different chain lengths had different influences on the efficiency of CPS in protecting BSA from the electric field-induced denaturation. SAMs with longer alkanethiol chain lengths were more efficient in protecting BSA from denaturation at negatively charged electrode surface than those formed by short-chain alkanethiols. Short alkanethiol SAMs could be prepared by co-adsorption with the protein on the electrode surface, which was not possible with the long-chain alkanethiols. CPS data were supported by impedance analysis. We believe that our work will be useful in the electrochemical sensing of nucleic acid-protein and protein-protein binding.
Workplace	Institute of Biophysics
Contact	Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244
Year of Publishing	2019

Number of the records: 1