Biomolecular Interactions of Novel Ruthenium(II) complexes with human serum albumin

Abstract

Ruthenium complexes occupied an important place in a group of transition metal complexes that were synthesized to replace platinum-based complexes and provide better selectivity and lower toxicity. This study involves creating three new ruthenium (η6-p-cymene) complexes with the formula [(η6-p-cym)Ru(O–O)Cl] using O,O-diketo ester ligands called ethyl 2-hydroxy-4-aryl-4-oxobut-2-enoate (1–3). The interactions with the blood transport protein HSA were studied to see how well the complexes could reach their target. The mentioned interactions were monitored by fluorescence spectroscopy with HSA alone and with the addition of the site markers Eosin Y (a marker for site I of subdomain IIA) and Ibuprofen (a marker for site II of subdomain IIIA). The site markers were used to precisely localize the binding site in the transported blood protein. The influence of bidentate ligands on binding efficacy was assessed by examining the calculated binding constants. Based on in vitro HSA experiments, complex 1 exhibited the highest HSA activity, suggesting that the presence of an alkene chain contributes to increased activity.