Determination of binding constants of human insulin complexes with serotonin, dopamine, arginine, and phenol by pressure assisted partial filling affinity capillary electrophoresis

0498027 - ÚOCHB 2019 RIV CZ eng C - Conference Paper (international conference)
Šolínová, Veronika - Žáková, Lenka - Jiráček, Jiří - Kašička, Václav
Determination of binding constants of human insulin complexes with serotonin, dopamine, arginine, and phenol by pressure assisted partial filling affinity capillary electrophoresis.
CECE 2018. 15th International Interdisciplinary Meeting on Bioanalysis. Brno: Ústav analytické chemie AV ČR, v. v. i., 2018 - (Foret, F.; Křenková, J.; Drobníková, I.; Klepárník, K.; Přikryl, J.), s. 272-275. ISBN 978-80-904959-5-1.
[CECE 2018. International Interdisciplinary Meeting on Bioanalysis /15./. Brno (CZ), 15.10.2018-17.10.2018]
R&D Projects: GA ČR(CZ) GA17-10832S; GA ČR(CZ) GA18-02597S
Institutional support: RVO:61388963
Keywords : human insulin * ligand * affinity capillary electrophoresis
OECD category: Analytical chemistry
http://www.ce-ce.org/user_uploads/program/CECE%202018%20Proceedings_WOS.pdf

A new method, pressure assisted partial filling affinity capillary electrophoresis (PF-ACE), has been developed to study noncovalent interactions of the hexamer of human insulin (HI) with cationic ligands, such as phenolic neurotransmitters serotonin and dopamine, and amino acid arginine, or with anionic ligand phenol, in alkaline aqueous solutions. The apparent binding constants, Kb, of the HI-ligand complexes were determined from the dependence of the effective migration time changes of the above ligands on the variable zone lengths of HI dissolved in the background electrolyte and hydrodynamically introduced into the bare fused silica capillary close to the UV detector. The HI interactions with the above ligands were found to be moderately strong, with Kb values in the range 385-1314 L/mol.
Permanent Link: http://hdl.handle.net/11104/0291135