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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Autor principal: Femia, A.L
Otros Autores: Temprana, C.F, Santos, J., Carbajal, M.L, Amor, M.S, Grasselli, M., Del Alonso, S.V
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2012
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-84871453073 
024 7 |2 cas  |a arsenic, 7440-38-2; fluorescein isothiocyanate, 25168-13-2, 27072-45-3, 3326-32-7; Arsenic, 7440-38-2; Arsenicals; Carrier Proteins; Fluorescein-5-isothiocyanate, 3326-32-7; Fluorescent Dyes; Thioredoxins, 52500-60-4; p-aminophenylarsine oxide 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
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100 1 |a Femia, A.L. 
245 1 3 |a An arsenic fluorescent compound as a novel probe to study arsenic-binding proteins 
260 |c 2012 
270 1 0 |m Del Alonso, S.V.; Laboratorio de Biomembranas, Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Peña 352, Bernal, B1876BXD Buenos Aires, Argentina; email: salonso@unq.edu.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a 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.  |l eng 
536 |a Detalles de la financiación: Universidad Nacional de Quilmes, PUNQ0396/07, UNQ-MPBio 53/1001 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, PIP 5832/05 
536 |a Detalles de la financiación: Ministerio de Ciencia, Tecnología e Innovación Productiva, PME 01730 
536 |a Detalles de la financiación: Acknowledgments We want to thank Dr. Gerardo Caballero for helpful discussions with mass spectra analyses, and to Lic Martín Noguera for his assistance with CD experiments. This work was supported by grants from Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET; PIP 5832/05) and Universidad Nacional de Quilmes (UNQ; UNQ-MPBio 53/1001(PUNQ0396/07), MINCyT (PME 01730). S del VA, MLC and MG are members of CONICET (Scientific Research Program) and IMBICE. Fellowships for ALF (CONICET, Posgrado T-I and II, D. No. Res. 1086/09), CFT (CONICET, Posgrado T-I and II, D. No. Res. 3100/08) and MSA (UNQ, No. Res. (CS) 113/07) are acknowledged. 
593 |a Laboratorio de Biomembranas, Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Peña 352, Bernal, B1876BXD Buenos Aires, Argentina 
593 |a Laboratorio de Inmunología y Virología, Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Peña 352, Bernal, B1876BXD Buenos Aires, Argentina 
593 |a Instituto de Bioquímica y Biofísica (IQUIFIB), Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires, Argentina 
593 |a LaMaBio, Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Saenz Peña 352, Bernal, B1876BXD Buenos Aires, Argentina 
690 1 0 |a ARSENIC CARCINOGENESIS 
690 1 0 |a CIRCULAR DICHROISM 
690 1 0 |a CONFORMATIONAL STUDIES 
690 1 0 |a DRUG DELIVERY SYSTEMS 
690 1 0 |a THIOREDOXIN 
690 1 0 |a 4 AMINOPHENYLARSINE OXIDE 
690 1 0 |a ARSENIC 
690 1 0 |a ARSENIC BINDING PROTEIN 
690 1 0 |a BINDING PROTEIN 
690 1 0 |a FLUORESCEIN ISOTHIOCYANATE 
690 1 0 |a FLUORESCENT DYE 
690 1 0 |a THIOREDOXIN 1 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a ARTICLE 
690 1 0 |a ATOMIC ABSORPTION 
690 1 0 |a CIRCULAR DICHROISM 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a FLUORESCENCE 
690 1 0 |a POLYACRYLAMIDE GEL ELECTROPHORESIS 
690 1 0 |a PROTEIN FOLDING 
690 1 0 |a PROTEIN INTERACTION 
690 1 0 |a PROTEIN STRUCTURE 
690 1 0 |a ARSENIC 
690 1 0 |a ARSENICALS 
690 1 0 |a CARRIER PROTEINS 
690 1 0 |a FLUORESCEIN-5-ISOTHIOCYANATE 
690 1 0 |a FLUORESCENT DYES 
690 1 0 |a KINETICS 
690 1 0 |a MODELS, MOLECULAR 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN CONFORMATION 
690 1 0 |a PROTEIN UNFOLDING 
690 1 0 |a SPECTRUM ANALYSIS 
690 1 0 |a TEMPERATURE 
690 1 0 |a THIOREDOXINS 
700 1 |a Temprana, C.F. 
700 1 |a Santos, J. 
700 1 |a Carbajal, M.L. 
700 1 |a Amor, M.S. 
700 1 |a Grasselli, M. 
700 1 |a Del Alonso, S.V. 
773 0 |d 2012  |g v. 31  |h pp. 656-666  |k n. 8  |p Protein J.  |x 15723887  |w (AR-BaUEN)CENRE-5767  |t Protein Journal 
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856 4 0 |u https://hdl.handle.net/20.500.12110/paper_15723887_v31_n8_p656_Femia  |y Handle 
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