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dc.contributor.author
Pacheco, Maria Emilia
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dc.contributor.author
Bruzzone, Liliana
dc.date.available
2019-05-08T20:19:47Z
dc.date.issued
2012-10
dc.identifier.citation
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
dc.identifier.issn
0022-2313
dc.identifier.uri
http://hdl.handle.net/11336/75910
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Bovine Serum Albumin
dc.subject
Fluorescence Quenching
dc.subject
Imazethapyr
dc.subject
Thermodynamic Parameters
dc.subject.classification
Otras Ciencias Químicas
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dc.subject.classification
Ciencias Químicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-05-03T17:37:09Z
dc.journal.volume
132
dc.journal.number
10
dc.journal.pagination
2730-2735
dc.journal.pais
Países Bajos
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dc.journal.ciudad
Amsterdam
dc.description.fil
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
dc.description.fil
Fil: Bruzzone, Liliana. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Química; Argentina
dc.journal.title
Journal of Luminescence
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0022231312003055
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jlumin.2012.05.023
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