INVESTIGADORES
VIZIOLI nora Matilde
congresos y reuniones científicas
Título:
Study of frataxin interaction with other proteins and metal ions by capillary electrophoresis
Autor/es:
COLLAZO, D; HERRERA, GEORGINA; SANTOS, J; VIZIOLI, NM
Lugar:
Santiago
Reunión:
Simposio; 22nd Latin-American Symposium on Biotechnology, Biomedical, Biopharmaceutical, and Industrial Applications of Capillary Electrophoresis and Microchip Technology; 2016
Resumen:
Human frataxin (FXN) has a vital role in the biosynthesis of iron-sulfur clusters (Fe-S), in mitochondria and its deficiency leads to a progressive neuromuscular degenerative disease known as Friedreich´s ataxia. FXN is a member of the Fe-S biosynthetic complex, since it physically and functionally interacts with other proteins of that complex.As an efficient and versatile technique for biomolecule analysis, capillary electrophoresis (CE) can help to elucidate protein-protein and metal-protein interactions. In this work, the interaction of FXN with iron and cobalt ions, and other proteins, such as ISCU and ISD11 was studied by CE under several conditions. Experiments were conducted using bare- and neutral coated-fused silica capillaries. Different background electrolyte composition (HEPES, TRIS, phosphate, and citrate solutions), pH, and additives were tested. CE analyses performed with 20 mmol/L TRIS solution at pH 7.4 as background electrolyte demonstrated that an increase of Fe (III) concentration in the FXN sample produced a decrease of free FXN fraction. Additionally, results from titration and nuclear magnetic resonance (NMR) indicated that FXN fixes iron and cobalt. The interaction of FXN with other proteins has been inferred from changes observed in the protein electrophoretic profile.As might be expected, the use of CE to characterize protein interaction with other proteins and metal ions in the context of the FXN characterization studies was of great value.