Determination of thermodynamic binding constants by affinity capillary electrophoresis

A strategy to study thermodynamic binding constants by affinity capillary electrophoresis (ACE) is presented. In order to simplify mathematical treatment, analogy with acid-base dissociation equilibrium is proposed: instead of ligand concentration [X], negative logarithm of ligand concentration (or...

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Autores principales: Lancioni, Carlina, Keunchkarian, Sonia, Castells, Cecilia Beatriz Marta, Gagliardi, Leonardo Gabriel
Formato: Articulo Preprint
Lenguaje:Inglés
Publicado: 2019
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/128708
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id I19-R120-10915-128708
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Thermodynamic binding constant
Affinity capillary electrophoresis
Chiral separation
Cyclodextrin
spellingShingle Química
Thermodynamic binding constant
Affinity capillary electrophoresis
Chiral separation
Cyclodextrin
Lancioni, Carlina
Keunchkarian, Sonia
Castells, Cecilia Beatriz Marta
Gagliardi, Leonardo Gabriel
Determination of thermodynamic binding constants by affinity capillary electrophoresis
topic_facet Química
Thermodynamic binding constant
Affinity capillary electrophoresis
Chiral separation
Cyclodextrin
description A strategy to study thermodynamic binding constants by affinity capillary electrophoresis (ACE) is presented. In order to simplify mathematical treatment, analogy with acid-base dissociation equilibrium is proposed: instead of ligand concentration [X], negative logarithm of ligand concentration (or activity), pX = -log[X], is used. On this base, and taking into account ionic activities, a general procedure for obtaining thermodynamic binding constants is proposed. In addition, the method provides electrophoretic mobilities of the free analyte and analyte-ligand complex, even when binding constants are low and thus, the complexed analyte fraction is also low. This is useful as a base to rationally analyze a diversity of situations, i.e., different mathematical dependencies are obtained when analytes and ligands with different charges are combined. Practical considerations are given for carrying out a full experimental design. Enantiomeric ACE separation based on the use of chiral selectors is addressed. 2-hydroxypropyl-β-cyclodextrin was chosen as a model ligand, and both enantiomeric forms of four pharmaceutical drugs (propranolol, pindolol, oxprenolol and homatropine methylbromide) were considered as model analytes. Practical aspects are detailed and thermodynamic binding constants as well as free and complexed analytes mobilities are determined.
format Articulo
Preprint
author Lancioni, Carlina
Keunchkarian, Sonia
Castells, Cecilia Beatriz Marta
Gagliardi, Leonardo Gabriel
author_facet Lancioni, Carlina
Keunchkarian, Sonia
Castells, Cecilia Beatriz Marta
Gagliardi, Leonardo Gabriel
author_sort Lancioni, Carlina
title Determination of thermodynamic binding constants by affinity capillary electrophoresis
title_short Determination of thermodynamic binding constants by affinity capillary electrophoresis
title_full Determination of thermodynamic binding constants by affinity capillary electrophoresis
title_fullStr Determination of thermodynamic binding constants by affinity capillary electrophoresis
title_full_unstemmed Determination of thermodynamic binding constants by affinity capillary electrophoresis
title_sort determination of thermodynamic binding constants by affinity capillary electrophoresis
publishDate 2019
url http://sedici.unlp.edu.ar/handle/10915/128708
work_keys_str_mv AT lancionicarlina determinationofthermodynamicbindingconstantsbyaffinitycapillaryelectrophoresis
AT keunchkariansonia determinationofthermodynamicbindingconstantsbyaffinitycapillaryelectrophoresis
AT castellsceciliabeatrizmarta determinationofthermodynamicbindingconstantsbyaffinitycapillaryelectrophoresis
AT gagliardileonardogabriel determinationofthermodynamicbindingconstantsbyaffinitycapillaryelectrophoresis
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