Probing the interaction of a new design oxali-palladium analogue with human serum albumin: A Spectroscopic Study

Protein-drug interactions are important in the pharmacokinetics of the drugs. Human serum albumin (HSA) is the most abundant protein fundamental of blood plasma and serves as a protein storage component. In the present study, the interaction of newly synthesized Pt(II) complex with HSA was studied using spectroscopic method of fluorescence at two temperatures of 25 and 37 °C. Analysis of the quenching mechanism via Stern-Volmer curve and determination of HSA binding parameters carried out using fluorescence data. Data analysis showed that dynamic mechanism has a main role in fluorescence quenching of has in the presence of complex. Also, the number of protein binding sites for complex indicated one binding site at two temperatures of 25 and 37 °C. According above results, we concluded that the new synthesized Pt(II) complex can bind to the blood carrier protein of HSA and change the structure of it which can be considered in design of new drugs.

Keywords:

HSA , Pt complex , Fluorescence , Binding site