The binding properties of two antitumor ruthenium(III) complexes to apotransferrin.
作者： F. Kratz , M. Hartmann , B. Keppler , L. Messori
DOI: 10.1016/S0021-9258(17)41984-3
关键词: Transferrin 、 Plasma protein binding 、 Metal 、 Binding site 、 Blood proteins 、 Medicinal chemistry 、 Stereochemistry 、 Adduct 、 Chemistry 、 Ruthenium 、 NAMI-A
摘要: The interaction of two ruthenium(III) complexes exhibiting high anticancer activity, namely trans-indazolium(bisindazole)tetrachlororuthenate(III) (ru-ind) and trans-imidazolium(bisimidazole)tetrachlororuthenate(III) (ru-im), with human serum apotransferrin has been investigated through spectroscopic chromatographic techniques the ultimate goal preparing adducts good selectivity for cancer cells. Whereas binding ru-im to takes several hours, ru-ind, less toxic complex, gives rise a well defined 2:1 complex within few minutes. We have ascertained that ru-ind occurs around iron sites; does not occur in absence bicarbonate, this anion dictates kinetic mechanistic characteristics protein ru-ind. do behave as iron(III) complexes, e.g. Fe(EDTA) or Fe(nitrilotriacetate), which lose their respective ligands when apotransferrin, but N-heterocycles remain attached metal protein-bound species. Reversion is obtained by acidification presence chelators such citrate ATP. In comparison cisplatin its deactivation proteins, our results indicate other could use transferrin drug delivery system. Furthermore, rapid seems be related lower toxicity while still antitumor activity.
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