An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins
Arsenic-binding proteins are under continuous research. Their identification and the elucidation of arsenic/ protein interaction mechanisms are important because the biological effects of these complexes may be related not only to arsenic but also to the arsenic/protein structure. Although many prot...
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2012
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15723887_v31_n8_p656_Femia http://hdl.handle.net/20.500.12110/paper_15723887_v31_n8_p656_Femia |
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paper:paper_15723887_v31_n8_p656_Femia2023-06-08T16:24:38Z An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins Arsenic carcinogenesis Circular dichroism Conformational studies Drug delivery systems Thioredoxin 4 aminophenylarsine oxide arsenic arsenic binding protein binding protein fluorescein isothiocyanate fluorescent dye thioredoxin 1 unclassified drug article atomic absorption circular dichroism enzyme activity fluorescence polyacrylamide gel electrophoresis protein folding protein interaction protein structure Arsenic Arsenicals Carrier Proteins Fluorescein-5-isothiocyanate Fluorescent Dyes Kinetics Models, Molecular Protein Binding Protein Conformation Protein Unfolding Spectrum Analysis Temperature Thioredoxins Arsenic-binding proteins are under continuous research. Their identification and the elucidation of arsenic/ protein interaction mechanisms are important because the biological effects of these complexes may be related not only to arsenic but also to the arsenic/protein structure. Although many proteins bearing a CXXC motif have been found to bind arsenic in vivo, new tools are necessary to identify new arsenic targets and allow research on protein/ arsenic complexes. In this work, we analyzed the performance of the fluorescent compound APAO-FITC (synthesized from p-aminophenylarsenoxide, APAO, and fluorescein isothiocyanate, FITC) in arsenic/protein binding assays using thioredoxin 1 (Trx) as an arsenic-binding protein model. The Trx-APAO-FITC complex was studied through different spectroscopic techniques involving UV-Vis, fluorescence, atomic absorption, infrared and circular dichroism. Our results show that APAO-FITC binds efficiently and specifically to the Trx binding site, labeling the protein fluorescently, without altering its structure and activity. In summary, we were able to study a protein/ arsenic complex model, using APAO-FITC as a labeling probe. The use of APAO-FITC in the identification of different protein and cell targets, as well as in in vivo biodistribution studies, conformational studies of arsenicbinding proteins, and studies for the design of drug delivery systems for arsenic anti-cancer therapies, is highly promising. © Springer Science+Business Media, LLC 2012. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15723887_v31_n8_p656_Femia http://hdl.handle.net/20.500.12110/paper_15723887_v31_n8_p656_Femia |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Arsenic carcinogenesis Circular dichroism Conformational studies Drug delivery systems Thioredoxin 4 aminophenylarsine oxide arsenic arsenic binding protein binding protein fluorescein isothiocyanate fluorescent dye thioredoxin 1 unclassified drug article atomic absorption circular dichroism enzyme activity fluorescence polyacrylamide gel electrophoresis protein folding protein interaction protein structure Arsenic Arsenicals Carrier Proteins Fluorescein-5-isothiocyanate Fluorescent Dyes Kinetics Models, Molecular Protein Binding Protein Conformation Protein Unfolding Spectrum Analysis Temperature Thioredoxins |
| spellingShingle |
Arsenic carcinogenesis Circular dichroism Conformational studies Drug delivery systems Thioredoxin 4 aminophenylarsine oxide arsenic arsenic binding protein binding protein fluorescein isothiocyanate fluorescent dye thioredoxin 1 unclassified drug article atomic absorption circular dichroism enzyme activity fluorescence polyacrylamide gel electrophoresis protein folding protein interaction protein structure Arsenic Arsenicals Carrier Proteins Fluorescein-5-isothiocyanate Fluorescent Dyes Kinetics Models, Molecular Protein Binding Protein Conformation Protein Unfolding Spectrum Analysis Temperature Thioredoxins An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins |
| topic_facet |
Arsenic carcinogenesis Circular dichroism Conformational studies Drug delivery systems Thioredoxin 4 aminophenylarsine oxide arsenic arsenic binding protein binding protein fluorescein isothiocyanate fluorescent dye thioredoxin 1 unclassified drug article atomic absorption circular dichroism enzyme activity fluorescence polyacrylamide gel electrophoresis protein folding protein interaction protein structure Arsenic Arsenicals Carrier Proteins Fluorescein-5-isothiocyanate Fluorescent Dyes Kinetics Models, Molecular Protein Binding Protein Conformation Protein Unfolding Spectrum Analysis Temperature Thioredoxins |
| description |
Arsenic-binding proteins are under continuous research. Their identification and the elucidation of arsenic/ protein interaction mechanisms are important because the biological effects of these complexes may be related not only to arsenic but also to the arsenic/protein structure. Although many proteins bearing a CXXC motif have been found to bind arsenic in vivo, new tools are necessary to identify new arsenic targets and allow research on protein/ arsenic complexes. In this work, we analyzed the performance of the fluorescent compound APAO-FITC (synthesized from p-aminophenylarsenoxide, APAO, and fluorescein isothiocyanate, FITC) in arsenic/protein binding assays using thioredoxin 1 (Trx) as an arsenic-binding protein model. The Trx-APAO-FITC complex was studied through different spectroscopic techniques involving UV-Vis, fluorescence, atomic absorption, infrared and circular dichroism. Our results show that APAO-FITC binds efficiently and specifically to the Trx binding site, labeling the protein fluorescently, without altering its structure and activity. In summary, we were able to study a protein/ arsenic complex model, using APAO-FITC as a labeling probe. The use of APAO-FITC in the identification of different protein and cell targets, as well as in in vivo biodistribution studies, conformational studies of arsenicbinding proteins, and studies for the design of drug delivery systems for arsenic anti-cancer therapies, is highly promising. © Springer Science+Business Media, LLC 2012. |
| title |
An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins |
| title_short |
An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins |
| title_full |
An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins |
| title_fullStr |
An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins |
| title_full_unstemmed |
An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins |
| title_sort |
arsenic fluorescent compound as a novel probe to study arsenic-binding proteins |
| publishDate |
2012 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15723887_v31_n8_p656_Femia http://hdl.handle.net/20.500.12110/paper_15723887_v31_n8_p656_Femia |
| _version_ |
1768543772235268096 |