Resumo

MARQUEZ, Maripaz; QUINTANAR, Liliana  e  CASTANEDA-HERNANDEZ, Gilberto. Spectroscopic characterization of Docetaxel binding to human serum albumin. Rev. mex. cienc. farm [online]. 2013, vol.44, n.1, pp.45-51. ISSN 1870-0195.

Docetaxel is an antineoplastic commercially called Taxotere. The union of Docetaxel to plasmatic proteins for its distribution is a critical step of the pharmacokinetics process that determines their adverse effects. The main plasma protein involved is human serum albumin (HSA). In this study, we evaluated the binding of Docetaxel to HSA using electronic absorption spectroscopy. The effects of incubation time after the addition of Docetaxel to HSA, reagents concentration and optical path length were evaluated. We concluded that the best conditions to evaluate Docetaxel-HSA interaction are: 4 to 28 µM of Docetaxel, 2 µM protein, without incubation of reagents, and using a 0.5 cm path length. In this work, we evaluated the binding of HSA to Docetaxel in Taxotere presentation, and the probe here developed could be applied to evaluate Docetaxel-HSA binding in different formulations.

Palavras-chave : spectroscopy; Docetaxel; plasma proteins.

        · resumo em Espanhol     · texto em Espanhol     · Espanhol ( pdf )