IQUIR   05412
INSTITUTO DE QUIMICA ROSARIO
Unidad Ejecutora - UE
artículos
Título:
INTERACTION OF THE COMPLEX [Ag(SULFADIMETOXINATE)] WITH BOVINE SERUM ALBUMIN (BSA)
Autor/es:
MONTI, L.; HURE, E.; MOSCONI, N.; PONTORIERO, A.; NERLI, V.; PICÓ, G.; ATRIA, ANA M.; CAMPAGNOLI, D.; RIZZOTTO, M.
Revista:
BIOCELL
Editorial:
INST HISTOL EMBRIOL-CONICET
Referencias:
Lugar: Mendoza; Año: 2010 vol. 34 p. 78 - 78
ISSN:
0327-9545
Resumen:
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Interaction
of the complex [Ag(sulfadimetoxinate)] with bovine
serum albumin (BSA)
1Monti,
Laura; 1Hure, E.; 1Mosconi, N.; 1Pontoriero, A.;
2Nerli, B.; 2Picó, G.; 3Atria, Ana M.; 4Campagnoli,
D.; 1Rizzotto, M.*
Áreas
1Inorgánica y 2Fisicoquímica, FCByF, UNR, Rosario, Argentina;
3Facultad de Ciencias Químicas y Farmacéuticas, Universidad de
Chile, Santiago, Chile; 4Facultad de Ingeniería Química, UNL, Santa
Fe, Argentina. E-mail: rizzotto@iquir-conicet.gov.ar
Binding of drugs to plasma
proteins is one of the factors that affect their availability in the human
body. Formation of complexes between sulfa drugs and metallic
ions is an extended field of research because it improves the action of the
sulfa drug. In the present work we studied the interaction of BSA with the
complex Ag-sulfadimetoxine (Ag-SDM). When aqueous solutions of silver nitrate and sodium
sulfadimetoxine (NaSDM) were mix a white solid was obtained, which was separated
and washed, in different experiences, with water or water and methanol. In both
cases the compound was solved in DMSO and later purified through crystallization
in a methanol camera. Elemental analysis (N, C, H, S and Ag) let us suggest
that all the solids were the same compound, with the following formula: [Ag(C12H13N4O4S].
In order to study the interaction of Ag-SDM with BSA, aqueous solutions of BSA
with and without ligand (Ag-SDM and initial drugs) were analyzed by UV-Vis
spectroscopy. An increment in absorbance and shifts to shorter wavelengths were
found with NaSDM and AgSDM. It was found a saturation effect with NaSDM and a possible
cooperative interaction with AgSDM. In conclusion, the formation of the complex
AgSDM could be produce changes in the mechanism of binding of NaSDM to BSA