The interaction studies of novel diaminophenazine gold(III) complex and Bovine Serum Albumin (BSA-ibuprofen and BSA-Eozine Y)

Abstract

It is well known that gold(III) complexes have found applications in medicinal inorganic chemistry. Considering this, the right choice of inert ligands in the structure of Au(III) complexes is crucial for predicting their properties and reactivity, especially towards biomolecules. Here are presented the results of the study of the interactions between the new gold(III) complex [Au(DAP)Cl3], with 2,3-diaminophenazine (DAP) as an inert ligand, and BSA. Specifically, serum albumin is the main soluble protein in the circulatory system of humans. The metabolism of drugs, their distribution, free concentration, and effectiveness strongly depend on the drug-albumin interaction. Investigation of the interactions of the [Au(DAP)Cl3] complex with bovine serum albumin (BSA) under physiological conditions was performed by fluorescence spectroscopy. This method was also used to identify the binding site on the BSA molecule, with eosin Y as a marker for site I (subdomain IIA), and ibuprofen as a marker for site II (subdomain IIIA). The results have shown that the complex moderately reacts with the BSA molecule with just one binding site for the complex on the protein. Additionally, based on the results with site markers, especially with eosin Y, it can be concluded that the studied complex binds to site I of the BSA molecule.