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Influence of redox activation of NAMI-A on affinity to serum proteins : transferrin and albumin
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dc.type
JournalArticle
pl
dc.description.physical
3181-3192
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dc.abstract.en
Imidazolium trans-tetrachloridodimethylsulfoxideimidazoleruthenate(III), NAMI-A, is a ruthenium drug exhibiting unique properties under clinical studies such as ability to inhibit the process of metastases without exerting tumor toxicity. Its place of action is concentrated at the extracellular level, therefore, the transformation and fate of this drug upon injection is of great importance. This study focuses on evaluation of the reducing potency of blood stream on interaction with two serum proteins: albumin and transferrin. It was investigated by applying various simplified serum models preserving physiological concentration of proteins and the amount of Ru complex as found in patients. It was shown that ruthenation of albumin is slightly increased while transferrin decreased upon addition of reductant in blood stream (ascorbate, glutathione, and cysteine) at physiological concentration. Interestingly, in serum models comprising low-molecular-mass components the amount of the reductant in the solution had a pronounced effect on the Ru content, in particular in transferrin. Supplementation of serum models with glutathione at concentration enough for complete reduction of NAMI-A selectively enhanced the binding of Ru complex to transferrin while ruthenation of albumin was almost unchanged. Spectrofluorimetric studies revealed that reduction has a marginal effect on binding affinity, therefore, both Ru(III) and (II) derivatives equally can compete for binding to transferrin.
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dc.subject.en
ELISA
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dc.subject.en
albumin
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dc.subject.en
ICP-MS
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dc.subject.en
transferrin
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dc.subject.en
reducing agents
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dc.subject.en
NAMI-A
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dc.description.volume
68
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dc.description.number
17-18
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dc.identifier.doi
10.1080/00958972.2015.1067692
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dc.identifier.eissn
1029-0389
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dc.title.journal
Journal of Coordination Chemistry
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dc.title.volume
Special Issue to Honour Professor Dr. Rudi van Eldik on the occasion of his 70th birthday
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dc.language.container
eng
pl
dc.affiliation
Wydział Chemii : Zakład Chemii Nieorganicznej
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dc.subtype
Article
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dc.rights.original
bez licencji
pl
.pointsMNiSW
[2015 A]: 25
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