Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis

Autores
Chanphai, P.; Cloutier, F; Oufqir, Y.; Leclerc, M. F.; Eijan, Ana Maria; Reyes Moreno, Carlos; Bérubé, G.; Tajmir Riahi, H. A.
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Two aminobenzoic acid derivatives DAB-0 and DAB-1 showed distinct biological properties on murine bladder cancer (BCa) cell line MB49-I. In contrast to DAB-1, DAB-0 does not possess any anti-inflammatory activity and is less toxic. Furthermore, DAB-0 does not interfere with INFγ-induced STAT1 activation and TNFα-induced IκB phosphorylation, while DAB-1 does. In order to rationalize these results, the binding efficacy of DAB-0 and DAB-1 with serum proteins such a human serum albumin (HSA), bovine serum albumin (BSA) and beta-lactoglobulin (β-LG) was investigated in aqueous solution at physiological pH. Multiple spectroscopic methods and thermodynamic analysis were used to determine the binding efficacy of DAB-0 and DAB-1 with serum proteins. Drug-protein conjugation was observed via through ionic contacts. DAB-1 forms stronger adducts than DAB-0, while β-LG shows more affinity with the order of stability β-LG > BSA > HSA. The stronger complexation of DAB-1 with serum proteins might account for its biological potential and transport in the blood. The binding efficacy ranged from 40 to 60%. Major alterations of protein secondary structures were detected upon drug complexation. Serum proteins are capable of delivering DAB-1 in vitro.
Fil: Chanphai, P.. Université du Québec a Montreal; Canadá
Fil: Cloutier, F. Université du Québec a Montreal; Canadá
Fil: Oufqir, Y.. Université du Québec a Montreal; Canadá
Fil: Leclerc, M. F.. Université du Québec a Montreal; Canadá
Fil: Eijan, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Reyes Moreno, Carlos. Université du Québec a Montreal; Canadá
Fil: Bérubé, G.. Université du Québec a Montreal; Canadá
Fil: Tajmir Riahi, H. A.. Université du Québec a Montreal; Canadá
Materia
BINDING EFFICACY
DAB-0
DAB-1
DELIVERY
SERUM PROTEIN
THERMODYNAMIC ANALYSIS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/150043
Acceder
id CONICETDig_745b4d308b916f0ef0bcc04b14c6744e
oai_identifier_str oai:ri.conicet.gov.ar:11336/150043
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysisChanphai, P.Cloutier, FOufqir, Y.Leclerc, M. F.Eijan, Ana MariaReyes Moreno, CarlosBérubé, G.Tajmir Riahi, H. A.BINDING EFFICACYDAB-0DAB-1DELIVERYSERUM PROTEINTHERMODYNAMIC ANALYSIShttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3Two aminobenzoic acid derivatives DAB-0 and DAB-1 showed distinct biological properties on murine bladder cancer (BCa) cell line MB49-I. In contrast to DAB-1, DAB-0 does not possess any anti-inflammatory activity and is less toxic. Furthermore, DAB-0 does not interfere with INFγ-induced STAT1 activation and TNFα-induced IκB phosphorylation, while DAB-1 does. In order to rationalize these results, the binding efficacy of DAB-0 and DAB-1 with serum proteins such a human serum albumin (HSA), bovine serum albumin (BSA) and beta-lactoglobulin (β-LG) was investigated in aqueous solution at physiological pH. Multiple spectroscopic methods and thermodynamic analysis were used to determine the binding efficacy of DAB-0 and DAB-1 with serum proteins. Drug-protein conjugation was observed via through ionic contacts. DAB-1 forms stronger adducts than DAB-0, while β-LG shows more affinity with the order of stability β-LG > BSA > HSA. The stronger complexation of DAB-1 with serum proteins might account for its biological potential and transport in the blood. The binding efficacy ranged from 40 to 60%. Major alterations of protein secondary structures were detected upon drug complexation. Serum proteins are capable of delivering DAB-1 in vitro.Fil: Chanphai, P.. Université du Québec a Montreal; CanadáFil: Cloutier, F. Université du Québec a Montreal; CanadáFil: Oufqir, Y.. Université du Québec a Montreal; CanadáFil: Leclerc, M. F.. Université du Québec a Montreal; CanadáFil: Eijan, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Medicina; ArgentinaFil: Reyes Moreno, Carlos. Université du Québec a Montreal; CanadáFil: Bérubé, G.. Université du Québec a Montreal; CanadáFil: Tajmir Riahi, H. A.. Université du Québec a Montreal; CanadáTaylor & Francis2021-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/150043Chanphai, P.; Cloutier, F; Oufqir, Y.; Leclerc, M. F.; Eijan, Ana Maria; et al.; Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis; Taylor & Francis; Journal Of Biomolecular Structure & Dynamics; 39; 1; 7-2021; 79-900739-1102CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1080/07391102.2020.1719889info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.1080/07391102.2020.1719889info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-05T09:50:07Zoai:ri.conicet.gov.ar:11336/150043instacron: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:34982025-11-05 09:50:07.5CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis
title Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis
spellingShingle Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis
Chanphai, P.
BINDING EFFICACY
DAB-0
DAB-1
DELIVERY
SERUM PROTEIN
THERMODYNAMIC ANALYSIS
title_short Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis
title_full Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis
title_fullStr Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis
title_full_unstemmed Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis
title_sort Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis
dc.creator.none.fl_str_mv Chanphai, P.
Cloutier, F
Oufqir, Y.
Leclerc, M. F.
Eijan, Ana Maria
Reyes Moreno, Carlos
Bérubé, G.
Tajmir Riahi, H. A.
author Chanphai, P.
author_facet Chanphai, P.
Cloutier, F
Oufqir, Y.
Leclerc, M. F.
Eijan, Ana Maria
Reyes Moreno, Carlos
Bérubé, G.
Tajmir Riahi, H. A.
author_role author
author2 Cloutier, F
Oufqir, Y.
Leclerc, M. F.
Eijan, Ana Maria
Reyes Moreno, Carlos
Bérubé, G.
Tajmir Riahi, H. A.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BINDING EFFICACY
DAB-0
DAB-1
DELIVERY
SERUM PROTEIN
THERMODYNAMIC ANALYSIS
topic BINDING EFFICACY
DAB-0
DAB-1
DELIVERY
SERUM PROTEIN
THERMODYNAMIC ANALYSIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Two aminobenzoic acid derivatives DAB-0 and DAB-1 showed distinct biological properties on murine bladder cancer (BCa) cell line MB49-I. In contrast to DAB-1, DAB-0 does not possess any anti-inflammatory activity and is less toxic. Furthermore, DAB-0 does not interfere with INFγ-induced STAT1 activation and TNFα-induced IκB phosphorylation, while DAB-1 does. In order to rationalize these results, the binding efficacy of DAB-0 and DAB-1 with serum proteins such a human serum albumin (HSA), bovine serum albumin (BSA) and beta-lactoglobulin (β-LG) was investigated in aqueous solution at physiological pH. Multiple spectroscopic methods and thermodynamic analysis were used to determine the binding efficacy of DAB-0 and DAB-1 with serum proteins. Drug-protein conjugation was observed via through ionic contacts. DAB-1 forms stronger adducts than DAB-0, while β-LG shows more affinity with the order of stability β-LG > BSA > HSA. The stronger complexation of DAB-1 with serum proteins might account for its biological potential and transport in the blood. The binding efficacy ranged from 40 to 60%. Major alterations of protein secondary structures were detected upon drug complexation. Serum proteins are capable of delivering DAB-1 in vitro.
Fil: Chanphai, P.. Université du Québec a Montreal; Canadá
Fil: Cloutier, F. Université du Québec a Montreal; Canadá
Fil: Oufqir, Y.. Université du Québec a Montreal; Canadá
Fil: Leclerc, M. F.. Université du Québec a Montreal; Canadá
Fil: Eijan, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Reyes Moreno, Carlos. Université du Québec a Montreal; Canadá
Fil: Bérubé, G.. Université du Québec a Montreal; Canadá
Fil: Tajmir Riahi, H. A.. Université du Québec a Montreal; Canadá
description Two aminobenzoic acid derivatives DAB-0 and DAB-1 showed distinct biological properties on murine bladder cancer (BCa) cell line MB49-I. In contrast to DAB-1, DAB-0 does not possess any anti-inflammatory activity and is less toxic. Furthermore, DAB-0 does not interfere with INFγ-induced STAT1 activation and TNFα-induced IκB phosphorylation, while DAB-1 does. In order to rationalize these results, the binding efficacy of DAB-0 and DAB-1 with serum proteins such a human serum albumin (HSA), bovine serum albumin (BSA) and beta-lactoglobulin (β-LG) was investigated in aqueous solution at physiological pH. Multiple spectroscopic methods and thermodynamic analysis were used to determine the binding efficacy of DAB-0 and DAB-1 with serum proteins. Drug-protein conjugation was observed via through ionic contacts. DAB-1 forms stronger adducts than DAB-0, while β-LG shows more affinity with the order of stability β-LG > BSA > HSA. The stronger complexation of DAB-1 with serum proteins might account for its biological potential and transport in the blood. The binding efficacy ranged from 40 to 60%. Major alterations of protein secondary structures were detected upon drug complexation. Serum proteins are capable of delivering DAB-1 in vitro.
publishDate 2021
dc.date.none.fl_str_mv 2021-07
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/11336/150043
Chanphai, P.; Cloutier, F; Oufqir, Y.; Leclerc, M. F.; Eijan, Ana Maria; et al.; Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis; Taylor & Francis; Journal Of Biomolecular Structure & Dynamics; 39; 1; 7-2021; 79-90
0739-1102
CONICET Digital
CONICET
url http://hdl.handle.net/11336/150043
identifier_str_mv Chanphai, P.; Cloutier, F; Oufqir, Y.; Leclerc, M. F.; Eijan, Ana Maria; et al.; Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis; Taylor & Francis; Journal Of Biomolecular Structure & Dynamics; 39; 1; 7-2021; 79-90
0739-1102
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1080/07391102.2020.1719889
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.1080/07391102.2020.1719889
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
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
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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score 13.082534

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