Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study

Autores
Pacheco, Maria Emilia; Bruzzone, Liliana
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The interaction between imazethapyr (IMA) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy. The Stern-Volmer quenching constant (K SV) at three temperatures was evaluated in order to determine the quenching mechanism. The dependence of fluorescence quenching on viscosity was also evaluated for this purpose. The results showed that IMA quenches the fluorescence intensity of BSA through a static quenching process. The values of the binding constant for the formed BSA-IMA complex and the number of binding sites were found to be 1.51×10 5 M -1 and 0.77, respectively, at room temperature. Based on the calculated thermodynamic parameters, the forces that dominate the binding process are hydrogen bonds and van der Waals forces, and the binding process is spontaneous and exothermic. The quenching of protein fluorescence by iodide ion was used to probe the accessibility of tryptophan residues in BSA and the change in accessibility induced by the presence of IMA. According to the obtained results, the BSA-IMA complex is formed in the site where the Trp-134 is located, causing it to become less exposed to the solvent. © 2012 Elsevier B.V. All rights reserved.
Fil: Pacheco, Maria Emilia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química; Argentina
Fil: Bruzzone, Liliana. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química; Argentina
Materia
Bovine Serum Albumin
Fluorescence Quenching
Imazethapyr
Thermodynamic Parameters
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:11336/75910
Acceder
id CONICETDig_8625aadafc292c45e2ac64d6a4fa3ec9
oai_identifier_str oai:ri.conicet.gov.ar:11336/75910
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric studyPacheco, Maria EmiliaBruzzone, LilianaBovine Serum AlbuminFluorescence QuenchingImazethapyrThermodynamic Parametershttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The interaction between imazethapyr (IMA) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy. The Stern-Volmer quenching constant (K SV) at three temperatures was evaluated in order to determine the quenching mechanism. The dependence of fluorescence quenching on viscosity was also evaluated for this purpose. The results showed that IMA quenches the fluorescence intensity of BSA through a static quenching process. The values of the binding constant for the formed BSA-IMA complex and the number of binding sites were found to be 1.51×10 5 M -1 and 0.77, respectively, at room temperature. Based on the calculated thermodynamic parameters, the forces that dominate the binding process are hydrogen bonds and van der Waals forces, and the binding process is spontaneous and exothermic. The quenching of protein fluorescence by iodide ion was used to probe the accessibility of tryptophan residues in BSA and the change in accessibility induced by the presence of IMA. According to the obtained results, the BSA-IMA complex is formed in the site where the Trp-134 is located, causing it to become less exposed to the solvent. © 2012 Elsevier B.V. All rights reserved.Fil: Pacheco, Maria Emilia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química; ArgentinaFil: Bruzzone, Liliana. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química; ArgentinaElsevier Science2012-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/75910Pacheco, Maria Emilia; Bruzzone, Liliana; Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study; Elsevier Science; Journal of Luminescence; 132; 10; 10-2012; 2730-27350022-2313CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0022231312003055info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jlumin.2012.05.023info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:06:17Zoai:ri.conicet.gov.ar:11336/75910instacron: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 10:06:17.665CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
title Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
spellingShingle Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
Pacheco, Maria Emilia
Bovine Serum Albumin
Fluorescence Quenching
Imazethapyr
Thermodynamic Parameters
title_short Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
title_full Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
title_fullStr Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
title_full_unstemmed Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
title_sort Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
dc.creator.none.fl_str_mv Pacheco, Maria Emilia
Bruzzone, Liliana
author Pacheco, Maria Emilia
author_facet Pacheco, Maria Emilia
Bruzzone, Liliana
author_role author
author2 Bruzzone, Liliana
author2_role author
dc.subject.none.fl_str_mv Bovine Serum Albumin
Fluorescence Quenching
Imazethapyr
Thermodynamic Parameters
topic Bovine Serum Albumin
Fluorescence Quenching
Imazethapyr
Thermodynamic Parameters
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 interaction between imazethapyr (IMA) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy. The Stern-Volmer quenching constant (K SV) at three temperatures was evaluated in order to determine the quenching mechanism. The dependence of fluorescence quenching on viscosity was also evaluated for this purpose. The results showed that IMA quenches the fluorescence intensity of BSA through a static quenching process. The values of the binding constant for the formed BSA-IMA complex and the number of binding sites were found to be 1.51×10 5 M -1 and 0.77, respectively, at room temperature. Based on the calculated thermodynamic parameters, the forces that dominate the binding process are hydrogen bonds and van der Waals forces, and the binding process is spontaneous and exothermic. The quenching of protein fluorescence by iodide ion was used to probe the accessibility of tryptophan residues in BSA and the change in accessibility induced by the presence of IMA. According to the obtained results, the BSA-IMA complex is formed in the site where the Trp-134 is located, causing it to become less exposed to the solvent. © 2012 Elsevier B.V. All rights reserved.
Fil: Pacheco, Maria Emilia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química; Argentina
Fil: Bruzzone, Liliana. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química; Argentina
description The interaction between imazethapyr (IMA) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy. The Stern-Volmer quenching constant (K SV) at three temperatures was evaluated in order to determine the quenching mechanism. The dependence of fluorescence quenching on viscosity was also evaluated for this purpose. The results showed that IMA quenches the fluorescence intensity of BSA through a static quenching process. The values of the binding constant for the formed BSA-IMA complex and the number of binding sites were found to be 1.51×10 5 M -1 and 0.77, respectively, at room temperature. Based on the calculated thermodynamic parameters, the forces that dominate the binding process are hydrogen bonds and van der Waals forces, and the binding process is spontaneous and exothermic. The quenching of protein fluorescence by iodide ion was used to probe the accessibility of tryptophan residues in BSA and the change in accessibility induced by the presence of IMA. According to the obtained results, the BSA-IMA complex is formed in the site where the Trp-134 is located, causing it to become less exposed to the solvent. © 2012 Elsevier B.V. All rights reserved.
publishDate 2012
dc.date.none.fl_str_mv 2012-10
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/11336/75910
Pacheco, Maria Emilia; Bruzzone, Liliana; Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study; Elsevier Science; Journal of Luminescence; 132; 10; 10-2012; 2730-2735
0022-2313
CONICET Digital
CONICET
url http://hdl.handle.net/11336/75910
identifier_str_mv Pacheco, Maria Emilia; Bruzzone, Liliana; Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study; Elsevier Science; Journal of Luminescence; 132; 10; 10-2012; 2730-2735
0022-2313
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/S0022231312003055
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jlumin.2012.05.023
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 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
_version_ 1842269951926206464
score 13.13397

Publicaciones similares