Impact of low- and high-molecular-mass components of human serum on NAMI-A binding to transferrin

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
K Śpiewak, M Brindell

Abstract

Imidazolium trans-tetrachloridodimethylsulfoxideimidazolruthenate(III), NAMI-A, a novel antimetastatic ruthenium complex was investigated towards affinity to transferrin (Tf), whether Tf-Ru adducts might be formed after its intravenous injection. Studies were focused on the holotransferrin due to its preferential binding to transferrin receptor. Here, we showed that holotransferrin is able to bind NAMI-A as readily as apotransferrin. The simulation of biological conditions of human serum performed by application of simplified serum models allowed to analyse ruthenium distribution between transferrin and albumin. The presence of physiological concentration of albumin (ca. 18-fold excess over Tf) resulted in a twofold decrease of ruthenium binding to Tf. Interestingly, the introducing of low-molecular-mass components of serum dramatically increased the ruthenation of Tf. Intermolecular competition binding studies between transferrin and albumin showed that both proteins bound similar amount of ruthenium species. Investigation of NAMI-A binding to Tf in human serum showed that this protein was not the major binding partner for Ru complex. However, in spite of many competing proteins still the ruthenation of Tf was observed. The la...Continue Reading

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Citations

Mar 8, 2016·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Pavel KasplerLothar Lilge
Feb 9, 2016·Dalton Transactions : an International Journal of Inorganic Chemistry·Dejan LazićAna Rilak
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Aug 14, 2019·Journal of Gastrointestinal Cancer·Hernán VillotaGiuliano Bernal

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Methods Mentioned

BETA
enzyme-linked immunosorbent assay
ELISA
electrophoresis
Fluorescence
X-ray
Affinity chromatography

Software Mentioned

PyMol

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