Resumen

ESPOSITO, Breno P.; OLIVEIRA, Elisabeth de; ZYNGIER, Szulim B.  y  NAJJAR, Renato. Effects of human serun albumin in some biological properties of rhodium(II) complexes. J. Braz. Chem. Soc. [online]. 2000, vol.11, n.5, pp. 447-452. ISSN 0103-5053.  http://dx.doi.org/10.1590/S0103-50532000000500003.

The affinities for human albumin (HSA) of five rhodium(II) complexes of general formula [Rh₂(bridge)₄] (bridge = acetate, propionate, butyrate, trifluoroacetate and trifluoroacetamidate) were determined by spectrophotometry. In the case of the alkylcarboxylates, an inverse correlation of affinity with their liposolubilities was observed. Diffusion of the free or protein-bound complexes into Ehrlich cells in vitro seems to be primarily governed by the hydrophobic character of the complex. The complex [Rh₂(tfc)₄] exhibited affinity towards the protein (K = 214.1) as well as cell partition both in the absence (32.1%) and presence (48.6%) of HSA. The compound HSA: [Rh₂(tfc)₄] has had its antitumoral action in tumor-bearing Balb-c mice investigated, showing that HSA can be a drug reservoir for the rhodium complex.

Palabras llave : rhodium; human serum albumin; binding constant; antitumor.