Pressure assisted partial filling affinity capillary electrophoresis employed for determination of binding constants of human insulin hexamer complexes with serotonin, dopamine, arginine, and phenol

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00501552" target="_blank" >RIV/61388963:_____/19:00501552 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0003267018313655?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0003267018313655?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.aca.2018.11.026" target="_blank" >10.1016/j.aca.2018.11.026</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Pressure assisted partial filling affinity capillary electrophoresis employed for determination of binding constants of human insulin hexamer complexes with serotonin, dopamine, arginine, and phenol

Popis výsledku v původním jazyce

A new method, pressure assisted partial filling affinity capillary electrophoresis, has been developed to study noncovalent molecular interactions of the hexamer of human insulin (HI) with biologically relevant ligands, basic phenolic neurotransmitters serotonin and dopamine, basic amino acid arginine, and very weakly acidic phenol, in alkaline aqueous media. The apparent binding constants, K-b, 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 hexamer dissolved in the background electrolyte (BGE) and hydrodynamically introduced into the bare fused silica capillary close to the UV detector. The strong cationic electroosmotic flow (EOF) in alkaline BGEs, 40/40 mM Tris/tricine, pH 8.1, and 25/34 mM NaOH/tricine, pH 8.5, with EOF mobilities 52.0 x 10(-9) and 58.0 x 10(-9) m(2)V(-1)s(-1), respectively, was reduced by the hydrodynamic counter flow induced by external pressure at the outlet capillary end to avoid expulsion of HI zone out of the capillary and to allow HI interaction with both cationic and anionic ligands inside the capillary. The HI hexamer interactions with the above ligands were found to be weak to moderately strong, with K-b values in the range 385-1314 L mol(-1), and decreasing in the order HIphenol > HI-dopamine > HI-serotonin > HI-arginine.

Název v anglickém jazyce

Pressure assisted partial filling affinity capillary electrophoresis employed for determination of binding constants of human insulin hexamer complexes with serotonin, dopamine, arginine, and phenol

Popis výsledku anglicky

A new method, pressure assisted partial filling affinity capillary electrophoresis, has been developed to study noncovalent molecular interactions of the hexamer of human insulin (HI) with biologically relevant ligands, basic phenolic neurotransmitters serotonin and dopamine, basic amino acid arginine, and very weakly acidic phenol, in alkaline aqueous media. The apparent binding constants, K-b, 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 hexamer dissolved in the background electrolyte (BGE) and hydrodynamically introduced into the bare fused silica capillary close to the UV detector. The strong cationic electroosmotic flow (EOF) in alkaline BGEs, 40/40 mM Tris/tricine, pH 8.1, and 25/34 mM NaOH/tricine, pH 8.5, with EOF mobilities 52.0 x 10(-9) and 58.0 x 10(-9) m(2)V(-1)s(-1), respectively, was reduced by the hydrodynamic counter flow induced by external pressure at the outlet capillary end to avoid expulsion of HI zone out of the capillary and to allow HI interaction with both cationic and anionic ligands inside the capillary. The HI hexamer interactions with the above ligands were found to be weak to moderately strong, with K-b values in the range 385-1314 L mol(-1), and decreasing in the order HIphenol > HI-dopamine > HI-serotonin > HI-arginine.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Analytica Chimica Acta

ISSN

0003-2670

e-ISSN

—

Svazek periodika

1052

Číslo periodika v rámci svazku

Apr 4

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

170-178

Kód UT WoS článku

000456436100019

EID výsledku v databázi Scopus

2-s2.0-85057043367