Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein

Autores
Challier, Cecilia; Beassoni, Paola Rita; Boetsch, Cristhian; Garcia, Norman Andino; Biasutti, Maria Alicia; Criado, Susana Noemi
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The complexity depicted by disease scenarios as diabetes mellitus, constitutes a very interesting field of study when drugs and biologically relevant components may be affected by such environments. In this report, the interaction between the protein Human Serum Albumin (HSA) and two antidiabetics (Andb), Gliclazide (Gli) and Glipizide (Glip) was studied through fluorescence and docking assays, in order to characterize these systems. On the basis that HSA and Andb can be exposed in vivo at high Reactive Oxygen Species (ROS) concentrations in diabetic patients, the degradative process of the protein free and bound to Andb, in presence of the species singlet molecular oxygen (O2(1Δg)), was evaluated. Fluorescence and docking assays indicated that Gli, as well as Glip bind to HSA on two sites, with binding constants values in the order of 104-105 M-1. Likewise, docking assays revealed that the location of Gli or Glip on the protein may be the HSA binding sites II and III. Thermodynamic parameters showed that the interaction between HSA and Glip is a favored, enthalpically-controlled process. Oxygen uptake experiments indicated that Glip is less photooxidizable than Gli through a O2(1Δg)-mediated process. Besides, the protein-Andb binding produced a decrease in the overall rate constant for O2(1Δg) quenching as compared to the value for the free protein. This fact could be interpreted in terms of a reduction in the availability of Tyrosine residues in the bonded protein, with a concomitant decrease in the physical quenching deactivation of the oxidative species.
Fil: Challier, Cecilia. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Beassoni, Paola Rita. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Boetsch, Cristhian. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Garcia, Norman Andino. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Biasutti, Maria Alicia. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Criado, Susana Noemi. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Binding
Docking
Gliclazide
Glipizide
Oxidative Stress
Human Serum Albumin
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/34413
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/34413
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the proteinChallier, CeciliaBeassoni, Paola RitaBoetsch, CristhianGarcia, Norman AndinoBiasutti, Maria AliciaCriado, Susana NoemiBindingDockingGliclazideGlipizideOxidative StressHuman Serum Albuminhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The complexity depicted by disease scenarios as diabetes mellitus, constitutes a very interesting field of study when drugs and biologically relevant components may be affected by such environments. In this report, the interaction between the protein Human Serum Albumin (HSA) and two antidiabetics (Andb), Gliclazide (Gli) and Glipizide (Glip) was studied through fluorescence and docking assays, in order to characterize these systems. On the basis that HSA and Andb can be exposed in vivo at high Reactive Oxygen Species (ROS) concentrations in diabetic patients, the degradative process of the protein free and bound to Andb, in presence of the species singlet molecular oxygen (O2(1Δg)), was evaluated. Fluorescence and docking assays indicated that Gli, as well as Glip bind to HSA on two sites, with binding constants values in the order of 104-105 M-1. Likewise, docking assays revealed that the location of Gli or Glip on the protein may be the HSA binding sites II and III. Thermodynamic parameters showed that the interaction between HSA and Glip is a favored, enthalpically-controlled process. Oxygen uptake experiments indicated that Glip is less photooxidizable than Gli through a O2(1Δg)-mediated process. Besides, the protein-Andb binding produced a decrease in the overall rate constant for O2(1Δg) quenching as compared to the value for the free protein. This fact could be interpreted in terms of a reduction in the availability of Tyrosine residues in the bonded protein, with a concomitant decrease in the physical quenching deactivation of the oxidative species.Fil: Challier, Cecilia. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Beassoni, Paola Rita. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Boetsch, Cristhian. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Garcia, Norman Andino. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Biasutti, Maria Alicia. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Criado, Susana Noemi. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Science2014-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/34413Challier, Cecilia; Beassoni, Paola Rita; Boetsch, Cristhian; Garcia, Norman Andino; Biasutti, Maria Alicia; et al.; Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein; Elsevier Science; Journal of Photochemistry and Photobiology B: Biology; 142; 11-2014; 20-281011-1344CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jphotobiol.2014.10.019info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1011134414003273info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:42:59Zoai:ri.conicet.gov.ar:11336/34413instacron: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:34982025-09-29 10:43:00.16CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
title Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
spellingShingle Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
Challier, Cecilia
Binding
Docking
Gliclazide
Glipizide
Oxidative Stress
Human Serum Albumin
title_short Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
title_full Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
title_fullStr Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
title_full_unstemmed Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
title_sort Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein
dc.creator.none.fl_str_mv Challier, Cecilia
Beassoni, Paola Rita
Boetsch, Cristhian
Garcia, Norman Andino
Biasutti, Maria Alicia
Criado, Susana Noemi
author Challier, Cecilia
author_facet Challier, Cecilia
Beassoni, Paola Rita
Boetsch, Cristhian
Garcia, Norman Andino
Biasutti, Maria Alicia
Criado, Susana Noemi
author_role author
author2 Beassoni, Paola Rita
Boetsch, Cristhian
Garcia, Norman Andino
Biasutti, Maria Alicia
Criado, Susana Noemi
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Binding
Docking
Gliclazide
Glipizide
Oxidative Stress
Human Serum Albumin
topic Binding
Docking
Gliclazide
Glipizide
Oxidative Stress
Human Serum Albumin
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The complexity depicted by disease scenarios as diabetes mellitus, constitutes a very interesting field of study when drugs and biologically relevant components may be affected by such environments. In this report, the interaction between the protein Human Serum Albumin (HSA) and two antidiabetics (Andb), Gliclazide (Gli) and Glipizide (Glip) was studied through fluorescence and docking assays, in order to characterize these systems. On the basis that HSA and Andb can be exposed in vivo at high Reactive Oxygen Species (ROS) concentrations in diabetic patients, the degradative process of the protein free and bound to Andb, in presence of the species singlet molecular oxygen (O2(1Δg)), was evaluated. Fluorescence and docking assays indicated that Gli, as well as Glip bind to HSA on two sites, with binding constants values in the order of 104-105 M-1. Likewise, docking assays revealed that the location of Gli or Glip on the protein may be the HSA binding sites II and III. Thermodynamic parameters showed that the interaction between HSA and Glip is a favored, enthalpically-controlled process. Oxygen uptake experiments indicated that Glip is less photooxidizable than Gli through a O2(1Δg)-mediated process. Besides, the protein-Andb binding produced a decrease in the overall rate constant for O2(1Δg) quenching as compared to the value for the free protein. This fact could be interpreted in terms of a reduction in the availability of Tyrosine residues in the bonded protein, with a concomitant decrease in the physical quenching deactivation of the oxidative species.
Fil: Challier, Cecilia. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Beassoni, Paola Rita. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Boetsch, Cristhian. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Garcia, Norman Andino. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Biasutti, Maria Alicia. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Criado, Susana Noemi. Universidad Nacional de Río Cuarto; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The complexity depicted by disease scenarios as diabetes mellitus, constitutes a very interesting field of study when drugs and biologically relevant components may be affected by such environments. In this report, the interaction between the protein Human Serum Albumin (HSA) and two antidiabetics (Andb), Gliclazide (Gli) and Glipizide (Glip) was studied through fluorescence and docking assays, in order to characterize these systems. On the basis that HSA and Andb can be exposed in vivo at high Reactive Oxygen Species (ROS) concentrations in diabetic patients, the degradative process of the protein free and bound to Andb, in presence of the species singlet molecular oxygen (O2(1Δg)), was evaluated. Fluorescence and docking assays indicated that Gli, as well as Glip bind to HSA on two sites, with binding constants values in the order of 104-105 M-1. Likewise, docking assays revealed that the location of Gli or Glip on the protein may be the HSA binding sites II and III. Thermodynamic parameters showed that the interaction between HSA and Glip is a favored, enthalpically-controlled process. Oxygen uptake experiments indicated that Glip is less photooxidizable than Gli through a O2(1Δg)-mediated process. Besides, the protein-Andb binding produced a decrease in the overall rate constant for O2(1Δg) quenching as compared to the value for the free protein. This fact could be interpreted in terms of a reduction in the availability of Tyrosine residues in the bonded protein, with a concomitant decrease in the physical quenching deactivation of the oxidative species.
publishDate 2014
dc.date.none.fl_str_mv 2014-11
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/11336/34413
Challier, Cecilia; Beassoni, Paola Rita; Boetsch, Cristhian; Garcia, Norman Andino; Biasutti, Maria Alicia; et al.; Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein; Elsevier Science; Journal of Photochemistry and Photobiology B: Biology; 142; 11-2014; 20-28
1011-1344
CONICET Digital
CONICET
url http://hdl.handle.net/11336/34413
identifier_str_mv Challier, Cecilia; Beassoni, Paola Rita; Boetsch, Cristhian; Garcia, Norman Andino; Biasutti, Maria Alicia; et al.; Interaction between Human Serum Albumin and antidiabetic compounds and its influence on the O2(1Δg)-mediated degradation of the protein; Elsevier Science; Journal of Photochemistry and Photobiology B: Biology; 142; 11-2014; 20-28
1011-1344
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jphotobiol.2014.10.019
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1011134414003273
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
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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score 13.070432

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