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

The result's identifiers

  • Result code in 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>

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10600 - Biological sciences

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2024

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Separation Science

  • ISSN

    1615-9306

  • e-ISSN

  • Volume of the periodical

    47

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    8

  • Pages from-to

    1-8

  • UT code for WoS article

    001140740000001

  • EID of the result in the Scopus database

    2-s2.0-85182196400