Interaction of the synthesized anticancer compound of the methyl-glycine 1,10-phenanthroline platinum nitrate with human serum albumin and human hemoglobin proteins by spectroscopy methods and molecular docking

摘要

In the present study, the interaction of the novel synthesized platinum complex named methyl-glycine 1,10-phenanthroline platinum nitrate product with two most crucial blood carrier proteins of hemoglobin (Hb) and human serum albumin (HSA) has been investigated. Notably, structural alternation ability of the above anticancer compound was assessed at various temperatures through multispectroscopic techniques such as far-UV circular dichroism (CD) and fluorescence with the participation of the molecular docking targeting Hb and HSA in the systems of the medicine delivery. Fluctuations in the inherent fluorescence intensities of the proteins in consequence of the Pt(II) complex binding represented statics of the quenching system. It should be mentioned that thermodynamic and binding parameters have been calculated through the analysis of the outcomes of the quenching and outcomes of van't Hoff equation for the two proteins. Theoretical and experimental findings pointed out that the leading force for the Pt(II) complex interaction was electrostatic for HSA and hydrophobic interactions for Hb. Moreover, fluorescence experiments discovered that one binding site would be available because of the Pt(II) complex binding in the two proteins accompanied by a negative Gibbs free energy value. Additionally, the far-UV CD outputs suggested that the Pt(II) complex would cause some variations in the regular secondary and tertiary structures of the HSA as the remarkable going down in the alpha helical contents of proteins structures at different temperatures equal to 25 degrees C and 37 degrees C; however, any noteworthy modifications have not been seen in the respective structures of Hb. However, the interaction between the newly made-up medicine (Pt(II) complex) and the two most crucial blood carrier proteins of the Hb and HSA made a notable shifting in the structures and conformations of the proteins via many fluctuations in the secondary and tertiary structures of the two proteins. Hence, such researches of designing the novel metal anticancer medicines may gather useful data for exploring the more suitable path in the face-off with severe disorders like various cancers through inventing and developing metal medical compounds that are more advantageous and have fewer consequences.