Jagiellonian University Repository

The reduction of (ImH)[trans-Ru^{III}Cl_4(dmso)(Im)] under physiological conditions : preferential reaction of the reduced complex with human serum albumin

The reduction of (ImH)[trans-Ru^{III}Cl_4(dmso)(Im)] ...

Show full item record

dc.contributor.author Brindell, Małgorzata [SAP11117158] pl
dc.contributor.author Stawoska, Iwona pl
dc.contributor.author Supel, Justyna [SAP12019544] pl
dc.contributor.author Skoczkowski, Andrzej pl
dc.contributor.author Stochel, Grażyna [SAP11011061] pl
dc.contributor.author van Eldik, Rudi [SAP14007947] pl
dc.date.accessioned 2014-12-23T14:36:35Z
dc.date.available 2014-12-23T14:36:35Z
dc.date.issued 2008 pl
dc.identifier.issn 0949-8257 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/2399
dc.language eng pl
dc.title The reduction of (ImH)[trans-Ru^{III}Cl_4(dmso)(Im)] under physiological conditions : preferential reaction of the reduced complex with human serum albumin pl
dc.type JournalArticle pl
dc.description.physical 909-918 pl
dc.abstract.en A systematic study of the reduction of (ImH)[trans-RuCl(4)(dmso)(Im)] (NAMI-A; dmso is dimethyl sulfoxide, Im is imidazole), a promising antimetastasing agent, by L-ascorbic acid under physiological conditions is reported. Under blood plasma conditions (pH 7.4, 0.1-0.15 M NaCl , 37 degrees C) the rapid reduction of trans-[Ru(III)Cl(4)(dmso)(Im)](-) results in the formation of trans-[Ru(II)Cl(4)(dmso)(Im)](2-) within seconds, and is followed by successive dissociation of the chloride ligands, whereas neither dmso nor imidazole ligands are released during the reaction. Under our experimental conditions, the formation of the ascorbate dianion is the rate-determining step, and once it has formed it reacts rapidly with NAMI-A. Moreover, the NAMI-A complex is very unstable at physiological pH (7.4); therefore, the hydrolysis of NAMI-A cannot be excluded as a competing reaction. During hydrolysis, aquated derivatives via stepwise dissociation of chloride and dmso ligands are formed, and most of these species have a higher redox potential and are expected to be even more easily reduced by ascorbic acid. Thus, it is very likely that the reduced form of NAMI-A or the reduction products of its hydrolytic derivatives react with albumin. The reaction of reduced NAMI-A with human serum albumin leads to the formation of stable adducts, with a binding efficiency very similar to that of the parent complex, viz., 3.2+/-0.3 and 4.0+/-0.4 mol of Ru(II) and Ru(III) per mole of albumin, respectively, however with a significantly higher reactivity. pl
dc.description.volume 2 pl
dc.description.number 6 pl
dc.identifier.doi 10.1007/s00775-008-0378-3 pl
dc.identifier.eissn 1432-1327 pl
dc.title.journal JBIC. Journal of Biological Inorganic Chemistry pl
dc.language.container eng pl
dc.affiliation Wydział Chemii : Zakład Chemii Nieorganicznej pl
dc.affiliation Pion Prorektora ds. badań naukowych i funduszy strukturalnych : Małopolskie Centrum Biotechnologii pl
dc.subtype Article pl

Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)