| Institution: | 1.Protein Chemistry Laboratory (PCL), Department of Biology,College of Sciences, Shiraz University,Shiraz,Iran;2.Institute of Biotechnology,Shiraz University,Shiraz,Iran;3.Department of Biotechnology, Faculty of Advanced Sciences and Technologies,University of Isfahan,Isfahan,Iran;4.Department of Chemistry, College of Sciences,Shiraz University,Shiraz,Iran;5.Department of Chemistry,Shiraz University of Technology,Shiraz,Iran;6.Department of Chemistry,Shahid Beheshti University, Evin, Tehran,Iran |
| Abstract: | Human serum albumin (HSA) primarily functions as a transport carrier for a vast variety of natural ligands and pharmaceutical drugs. In the present study, three structurally related cationic Pt(II) complexes (Pt(ppy)(dppe)]CF3CO2: 1, Pt(bhq)(dppe)]CF3CO2: 2, and Pt(bhq)(dppf)]CF3CO2: 3) were used to evaluate their interaction with HSA under different experimental setups, using UV–Vis absorption spectroscopy, fluorescence and circular dichroism techniques. The spectroscopic results suggest that upon binding to HSA, the Pt(II) complexes could effectively induce structural alteration of the protein. The complexes can bind to HSA with the binding affinities of the following order: 3 > 2 > 1. Also, thermodynamic parameters of binding between these complexes and HSA indicated the existence of entropy-driven spontaneous interaction which primarily dominated with the hydrophobic forces. Also, docking simulation study revealed the binding details of these complexes on HSA. Complex 3 with highest binding affinity for HSA indicates lowest denaturing effect on this protein. The low denaturation properties of 3 appear important in the terms of lower susceptibility of this platinum complex for possible development of deleterious side effects. |
