Determination of thermodynamic binding constants by affinity capillary electrophoresis
- Autores
- Lancioni, Carlina; Keunchkarian, Sonia; Castells, Cecilia Beatriz Marta; Gagliardi, Leonardo Gabriel
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
Fil: Lancioni, Carlina. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química. Grupo Cromatografía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Keunchkarian, Sonia. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química. Grupo Cromatografía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Castells, Cecilia Beatriz Marta. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Gagliardi, Leonardo Gabriel. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina - Materia
-
AFFINITY CAPILLARY ELECTROPHORESIS
CHIRAL SEPARATION
CYCLODEXTRIN
THERMODYNAMIC BINDING CONSTANT - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/117271
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Determination of thermodynamic binding constants by affinity capillary electrophoresisLancioni, CarlinaKeunchkarian, SoniaCastells, Cecilia Beatriz MartaGagliardi, Leonardo GabrielAFFINITY CAPILLARY ELECTROPHORESISCHIRAL SEPARATIONCYCLODEXTRINTHERMODYNAMIC BINDING CONSTANThttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1A 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.Fil: Lancioni, Carlina. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química. Grupo Cromatografía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Keunchkarian, Sonia. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química. Grupo Cromatografía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Castells, Cecilia Beatriz Marta. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Gagliardi, Leonardo Gabriel. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaElsevier Science2019-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/117271Lancioni, Carlina; Keunchkarian, Sonia; Castells, Cecilia Beatriz Marta; Gagliardi, Leonardo Gabriel; Determination of thermodynamic binding constants by affinity capillary electrophoresis; Elsevier Science; Talanta; 192; 1-2019; 448-4540039-9140CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0039914018309548info:eu-repo/semantics/altIdentifier/doi/10.1016/j.talanta.2018.09.044info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:40Zoai:ri.conicet.gov.ar:11336/117271instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:44:40.403CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Determination of thermodynamic binding constants by affinity capillary electrophoresis |
title |
Determination of thermodynamic binding constants by affinity capillary electrophoresis |
spellingShingle |
Determination of thermodynamic binding constants by affinity capillary electrophoresis Lancioni, Carlina AFFINITY CAPILLARY ELECTROPHORESIS CHIRAL SEPARATION CYCLODEXTRIN THERMODYNAMIC BINDING CONSTANT |
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 |
dc.creator.none.fl_str_mv |
Lancioni, Carlina Keunchkarian, Sonia Castells, Cecilia Beatriz Marta Gagliardi, Leonardo Gabriel |
author |
Lancioni, Carlina |
author_facet |
Lancioni, Carlina Keunchkarian, Sonia Castells, Cecilia Beatriz Marta Gagliardi, Leonardo Gabriel |
author_role |
author |
author2 |
Keunchkarian, Sonia Castells, Cecilia Beatriz Marta Gagliardi, Leonardo Gabriel |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
AFFINITY CAPILLARY ELECTROPHORESIS CHIRAL SEPARATION CYCLODEXTRIN THERMODYNAMIC BINDING CONSTANT |
topic |
AFFINITY CAPILLARY ELECTROPHORESIS CHIRAL SEPARATION CYCLODEXTRIN THERMODYNAMIC BINDING CONSTANT |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
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. Fil: Lancioni, Carlina. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química. Grupo Cromatografía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Keunchkarian, Sonia. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química. Grupo Cromatografía; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Castells, Cecilia Beatriz Marta. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Gagliardi, Leonardo Gabriel. Universidad Nacional de la Plata. Facultad de Cs.exactas. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos. - Comision de Investigaciones Cientificas de la Provincia de Buenos Aires. Laboratorio de Investigacion y Desarrollo de Metodos Analiticos.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina |
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. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-01 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/117271 Lancioni, Carlina; Keunchkarian, Sonia; Castells, Cecilia Beatriz Marta; Gagliardi, Leonardo Gabriel; Determination of thermodynamic binding constants by affinity capillary electrophoresis; Elsevier Science; Talanta; 192; 1-2019; 448-454 0039-9140 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/117271 |
identifier_str_mv |
Lancioni, Carlina; Keunchkarian, Sonia; Castells, Cecilia Beatriz Marta; Gagliardi, Leonardo Gabriel; Determination of thermodynamic binding constants by affinity capillary electrophoresis; Elsevier Science; Talanta; 192; 1-2019; 448-454 0039-9140 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0039914018309548 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.talanta.2018.09.044 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.13397 |