Contactless conductivity detector as a tool for improving universality and sensitivity of capillary electrophoresis-frontal analysis: Proof of concept

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F24%3A00135292" target="_blank" >RIV/00216224:14310/24:00135292 - isvavai.cz</a>

Výsledek na webu

<a href="https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/jssc.202300667" target="_blank" >https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/jssc.202300667</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/jssc.202300667" target="_blank" >10.1002/jssc.202300667</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Contactless conductivity detector as a tool for improving universality and sensitivity of capillary electrophoresis-frontal analysis: Proof of concept

Popis výsledku v původním jazyce

Drug binding to plasma proteins influences processes such as liberation, adsorption, disposition, metabolism and elimination of drugs, which are thus one of the key steps of a new drug development. As a result, the characterization of drug protein interactions is an essential part of these time- and money-consuming processes. It is important to determine not only the binding strength and the stoichiometry of interaction, but also the binding site of a drug on a protein molecule, because two drugs with the same binding site can mutually affect free drug concentration. Capillary electrophoresis-frontal analysis with mobility shift affinity capillary electrophoresis is one of the most used affinity CE methods for the characterization of these interactions. In this study, a well-known sensitivity problem of most capillary electrophoresis-frontal analyses using UV detection is solved by its combination with contactless conductivity detection, which provided 6-fold lower limits of quantitation and detection. Binding parameters of the human serum albumin salicylic acid model affinity pair were evaluated by this newly developed approach and by the classical approach with UV detection primarily used for their mutual comparison. The results of both approaches agreed well, and are also in agreement with literature data obtained using different techniques.

Název v anglickém jazyce

Contactless conductivity detector as a tool for improving universality and sensitivity of capillary electrophoresis-frontal analysis: Proof of concept

Popis výsledku anglicky

Drug binding to plasma proteins influences processes such as liberation, adsorption, disposition, metabolism and elimination of drugs, which are thus one of the key steps of a new drug development. As a result, the characterization of drug protein interactions is an essential part of these time- and money-consuming processes. It is important to determine not only the binding strength and the stoichiometry of interaction, but also the binding site of a drug on a protein molecule, because two drugs with the same binding site can mutually affect free drug concentration. Capillary electrophoresis-frontal analysis with mobility shift affinity capillary electrophoresis is one of the most used affinity CE methods for the characterization of these interactions. In this study, a well-known sensitivity problem of most capillary electrophoresis-frontal analyses using UV detection is solved by its combination with contactless conductivity detection, which provided 6-fold lower limits of quantitation and detection. Binding parameters of the human serum albumin salicylic acid model affinity pair were evaluated by this newly developed approach and by the classical approach with UV detection primarily used for their mutual comparison. The results of both approaches agreed well, and are also in agreement with literature data obtained using different techniques.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10600 - Biological sciences

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)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

Journal of Separation Science

ISSN

1615-9306

e-ISSN

—

Svazek periodika

47

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

8

Strana od-do

1-8

Kód UT WoS článku

001140740000001

EID výsledku v databázi Scopus

2-s2.0-85182196400