Interaction of Cis- and Trans-RuCl2(DMSO)4 with Human Serum Albumin
2000
Interaction of Ruthenium Complexes with Human Serum Albumin
publication
Evidence: moderate
Author Information
Author(s): Lilianna Trynda-Lemiesz, Henryk Kozlowski, Nikolas Katsaros
Primary Institution: Faculty of Chemistry, University of Wroclaw
Hypothesis
How do cis- and trans-RuCl2(DMSO)4 complexes interact with human serum albumin?
Conclusion
The study shows that both cis- and trans-RuCl2(DMSO)4 complexes bind to human serum albumin, causing significant conformational changes in the protein.
Supporting Evidence
- Albumin can specifically bind one mole of the cis-isomer and two moles of the trans-isomer RuCl2(DMSO)4 complex.
- The interaction of RuCl2(DMSO)4 with HSA causes a conformational change with the loss of helical stability of the protein.
- The binding of trans-isomer to HSA was found to be more effective than that of the cis-isomer.
Takeaway
This study looks at how two types of metal drugs interact with a protein in our blood, which helps us understand how these drugs work in the body.
Methodology
The interaction was studied using UV-Vis, circular dichroism, fluorescence spectroscopy, and ICP(AES) methods.
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