Počet záznamů: 1
Chronopotentiometric sensing of specific interactions between lysozyme and the DNA aptamer
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SYSNO ASEP 0476545 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Chronopotentiometric sensing of specific interactions between lysozyme and the DNA aptamer Tvůrce(i) Ostatná, Veronika (BFU-R) RID, ORCID
Vargová, Veronika (BFU-R)
Kekedy-Nagy, L. (DK)
Černocká, Hana (BFU-R) RID, ORCID
Ferapontova, E.E. (DK)Celkový počet autorů 5 Zdroj.dok. Bioelectrochemistry. - : Elsevier - ISSN 1567-5394
Roč. 114, APR2017 (2017), s. 42-47Poč.str. 6 s. Forma vydání Tištěná - P Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova self-assembled monolayers ; protein interactions ; lysozyme Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology CEP GA13-00956S GA ČR - Grantová agentura ČR Institucionální podpora BFU-R - RVO:68081707 UT WOS 000394073500006 DOI 10.1016/j.bioelechem.2016.12.003 Anotace Specific DNA-protein interactions are vital for cellular life maintenance processes, such as transcriptional regulation, chromosome maintenance, replication and DNA repair, and their monitoring gives valuable information on molecular-level organization of those processes. Here, we propose a new method of label-free electrochemical sensing of sequence specific binding between the lysozyme protein and a single stranded DNA aptamer specific for lysozyme (DNA(apta)) that exploits the constant current chronopotentiometric stripping (CPS) analysis at modified mercury electrodes. Specific lysozyme-DNA(apta) binding Was distinguished from nonspecific lysozyme-DNA interactions at thioglycolic acid-modified mercury electrodes, but not at the dithiothreitol-modified or bare mercury electrodes. Stability of the surface-attached lysozyme-DNA(apta), layer depended on the stripping current (I-str) intensity, suggesting that the integrity of the layer critically depends on the time of its exposure to negative potentials. Stabilities of different lysozyme-DNA complexes at the negatively polarized electrode surface were tested, and it was shown that structural transitions of the specific lysozyme-DNA(apta) complexes occur in the I-str ranges different from those observed for assemblies of lysozyme with DNA sequences capable of only nonspecific lysozyme-DNA interactions. Thus, the CPS allows distinct discrimination between specific and non-specific protein-DNA binding and provides valuable information on stability of the nucleic acid-protein interactions at the polarized interfaces. (C) 2016 Elsevier B.V. All rights reserved. Pracoviště Biofyzikální ústav Kontakt Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Rok sběru 2018
Počet záznamů: 1