Multi-spectroscopic studies of the interaction of new synthesized platin complex with human carrier protein of serum albumin.

Previous reports have shown that protein-drug interaction helps to improve the pharmacokinetics of the drugs. Human serum albumin (HSA) is one of the basic components of blood plasma and it serves as a storage and carrier protein. In the present study, the interaction of a new synthesized Pt [iso]2 complex (cis - [Pt(NH-Isopentylamine)(Isopentylglycine)]NO with HSA was studied using the spectroscopic methods of fluorescence and circular dichroic (CD) at two different temperatures of 25 and 37 °C. Analysis of the quenching mechanism via Stern-Volmer curve, determination of HSA binding parameters (0.65 × 10 and 2.27 × 10) and standard Gibbs free energy (-25.8, and 21.77) at 25 and 37 °C, respectively, carried out using fluorescence quenching data. Data analysis showed that the static mechanism has the main role in fluorescence quenching. Also, the number of protein binding sites for complex indicated one binding site at two temperatures of 25 and 37 °C. The secondary structure of protein in the presence of different concentrations of Pt(II) complex did not show any significant alterations. Whereas, thermal stability of the HSA was reduced in the presence of complex. Also, thermal analysis obtained the values of ΔG° for HSA and HSA in presence of Pt [Iso] 20, 13, respectively. According to the above results, we concluded that the new synthesized Pt complex can bind to the blood carrier protein of HSA and change the stability of it which can be considered in the design of new drugs.Communicated by Ramaswamy H. Sarma.