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Synthesis, characterization, and binding assessment with human serum albumin of three bipyridine lanthanide(III) complexes
In this work, the terbium(III), dysprosium(III), and ytterbium(III) complexes containing 2, 2?-bipyridine (bpy) ligand have been synthesized and characterized using CHN elemental analysis, FT-IR, UV?Vis and 1H-NMR techniques and their binding behavior with human serum albumin (HSA) was studied by UV?Vis, fluorescence and molecular docking examinations. The experimental data indicated that all three lanthanide complexes have high binding affinity to HSA with effective quenching of HSA fluorescence via static mechanism. The binding parameters, the type of interaction, the value of resonance energy transfer, and the binding distance between complexes and HSA were estimated from the analysis of fluorescence measurements and Foerster theory. The thermodynamic parameters suggested that van der Waals interactions and hydrogen bonds play an important role in the binding mechanism. While, the energy transfer from HSA molecules to all these complexes occurs with high probability, the order of binding constants (BpyTb?>?BpyDy?>?BpyYb) represents the importance of radius of Ln3+ ion in the complex-HSA interaction. The results of molecular docking calculation and competitive experiments assessed site 3 of HSA, located in subdomain IB, as the most probable binding site for these ligands and also indicated the microenvironment residues around the bound mentioned complexes. The computational results kept in good agreement with experimental data.
Synthesis, characterization, and binding assessment with human serum albumin of three bipyridine lanthanide(III) complexes
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Reference£º
Iron Catalysis in Organic Synthesis | Chemical Reviews,
Iron Catalysis in Organic Synthesis: A Critical Assessment of What It Takes To Make This Base Metal a Multitasking Champion