Article
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY  (2006)

Nitrofurylsemicarbazone Rhenium and Ruthenium Complexes as Anti-trypanosomal Agents

Otero L.; Gambino D.; Aguirre, G.; Boiani, L; Gonzalez, M.; Cerecetto, H.; Denicola, A; Rigol, C; Olea Azar C.; Maya J.D.; Morello A.

Keywords: oxidation, chemistry, ruthenium, spectroscopy, stability, electron, electrochemistry, reduction, animals, synthesis, binding, metal, complex, serum, protein, trypanosoma, spin, mass, ligand, rhenium, resonance, agents, compound, parasite, atom, nuclear, bovine, agent, radical, infrared, albumin, spectrophotometry, formation, organometallic, drug, article, hydrophilicity, spectrometry, activity, cruzi, bombardment, magnetic, controlled, nitrofuran, nitrofurans, animal, antiprotozoal, semicarbazone, study, compounds, derivative, Reaction, nonhuman, effect, biological, Free, Spectrophotometry,, Spectrometry,, solution, antitrypanosomal, Trypanocidal, aqueous, fast, Mass,, Semicarbazones

Abstract

Rhenium and ruthenium complexes of the type [Re VOCl 2(PPh 3)L] and [Ru IICl 2(DMSO) 2L], where L are 5-nitrofurylsemicarbazone derivatives, were prepared in an effort to obtain new anti-trypanosomal agents combining the recognized biological activity of these metals and the trypanocidal activity of the free ligands. Rhenium complexes resulted unstable in aqueous solution not allowing their use as potential drugs. On the other hand, complexation to ruthenium of the bioactive ligands lead to the lack of antiprotozoa activity even though free radical production and redox cycling induction were detected when the compounds were incubated in presence of Trypanosoma cruzi cells. The lack of anti-trypanosomal activity of ruthenium complexes could be explained on the basis of their high protein binding capacity and their high hydrophilicity. © 2006.

Más información

Título de la Revista: EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
Volumen: 41
Número: 11
Editorial: ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Fecha de publicación: 2006
Página de inicio: 1231
Página final: 1239
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-33750523995&partnerID=q2rCbXpz