Electrochemical sensing of interaction of anterior gradient-2 protein with peptides at a charged interface

0492336 - BFÚ 2019 RIV GB eng J - Článek v odborném periodiku
Ostatná, Veronika - Kasalová, Veronika - Sommerová, L. - Hrstka, R.
Electrochemical sensing of interaction of anterior gradient-2 protein with peptides at a charged interface.
Electrochimica acta. Roč. 269, APR 10 2018 (2018), s. 70-75. ISSN 0013-4686. E-ISSN 1873-3859
Grant CEP: GA ČR GA15-21855S; GA MŠMT EF15_003/0000477
Institucionální podpora: RVO:68081707
Klíčová slova: mercury-electrodes * aptamers * therapeutics * evolution
Obor OECD: Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)
Impakt faktor: 5.383, rok: 2018

Anterior gradient-2 protein (AGR2) is overexpressed in many human cancers, and this protein presents a novel promising cancer biomarker. We show significant progress in understanding of the electric field effects on AGR2-peptides complexes using constant current chronopotentiometric stripping (CPS) analysis. Surface-attached AGR2-peptide complexes can be disintegrated as a result of their exposure to negative potentials. By controlling the exposure time and temperature, peaks of weakly bound nonspecific complexes can be discriminated from tightly bound specific complexes. Using CPS analysis we found that mutant E60A-AGR2 forms weaker complex with peptide aptamer in comparison to wild type AGR2. These data highlight the utility of this method for studying real-time dynamics of surface-attached protein-peptide complexes. (C) 2018 Elsevier Ltd. All rights reserved.
Trvalý link: http://hdl.handle.net/11104/0285858