Negligible interaction of [Ru(Phen)3]2+ with human serum albumin makes it promising for a reliable in vivo assessment of the tissue oxygenation
| Autor: | Michal Nemergut, Daniel Jancura, Veronika Huntosova, Zuzana Jurasekova, Dominik Belej, Georges Wagnières |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Stereochemistry Phenanthroline Serum albumin chemistry.chemical_element 010402 general chemistry 01 natural sciences Biochemistry Oxygen Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound medicine biology Chemistry Human serum albumin Blood proteins 0104 chemical sciences Ruthenium 030104 developmental biology embryonic structures biology.protein Limiting oxygen concentration Luminescence Nuclear chemistry medicine.drug |
| Zdroj: | Journal of Inorganic Biochemistry. 174:37-44 |
| ISSN: | 0162-0134 |
| DOI: | 10.1016/j.jinorgbio.2017.05.016 |
| Popis: | The interaction between a ruthenium - based water soluble oxygen probe ([Ru(Phen)3]2+, phen - phenanthroline) and human serum albumin (HSA) was investigated with the aim of describing the influence of HSA on the [Ru(Phen)3]2+ luminescence properties. Nowadays, several oxygen sensitive luminescent probes are used to determine the oxygen level in different compartments of living organisms. However, they can interact, depending on their hydrophilic/hydrophobic characters, with various serum proteins, and/or lipids, during their utilization for invivo oxygen measurement. Since HSA is the most abundant serum protein in most biological organisms, its presence may affect the spectral properties of the employed probes and, consequently, the determination of the oxygen concentration. Having this in mind, we have applied several spectroscopic and calorimetric techniques to study [Ru(Phen)3]2+ - HSA mixtures. Only a negligible effect of HSA on the absorption and luminescence spectra of [Ru(Phen)3]2+ was observed. In addition, differential scanning calorimetric studies showed that [Ru(Phen)3]2+ does not significantly influence HSA thermal stability. Importantly, [Ru(Phen)3]2+ retained a reliable luminescence lifetime sensitivity to the oxygen concentration in solutions supplemented with HSA and in U87 MG cancer cells. Finally, the biodistribution of [Ru(Phen)3]2+ in the presence of serum proteins in the blood stream of chick embryo's chorioallantoic membrane (CAM) was investigated. Fast [Ru(Phen)3]2+ and similar extravasations were observed in the presence or absence of CAM-serum. We can conclude that HSA-[Ru(Phen)3]2+ complex interaction does not significantly influence the potential of [Ru(Phen)3]2+ to be a suitable candidate for a reliable oxygen probe in living organisms. |
| Databáze: | OpenAIRE |
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