Synthesis, characterization, and binding assessment with human serum albumin of three bipyridine lanthanide(III) complexes

Abstract

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 H-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 Förster 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 Ln 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.

New transition metal complexes of 9,10‐phenanthrenequinone p‐toluyl hydrazone Schiff base: Synthesis, spectroscopy, DNA and HSA interactions, antimicrobial, DFT and docking studies

“…Fluorescence energy transfer happens via overlapping of the emission spectrum of a fluorophore (donor, HSA) with the absorption spectrum of a molecule (acceptor, Schiff base compound) . The overlap of the absorption spectra of synthesized compounds with the fluorescence emission spectra of HSA is shown in Figure .…”

In vitro anticancer activity of parent and nano-encapsulated samarium(iii) complex towards antimicrobial activity studies and FS-DNA/BSA binding affinity

“…8 Furthermore, serum albumins are the most abundant protein in blood that show signicant role in the distribution, metabolism, and transport of various exogenous compounds (containing drugs, amino acids, fatty acids, and pharmaceuticals). 10 In continuation of recent research work, [11][12][13][14][15][16][17] the synthesis, characterization, and interaction of the Sm-complex, [Sm(bpy) 2 Cl 3 (OH 2 )] (Scheme 1), with FS-DNA and BSA by different types of experimental techniques and docking calculation are reported in this paper. Moreover, the parent, lipid nano-encapsulated (LNEP) and starch nano-encapsulated Scheme 1 Chemical structure of the Sm-complex.…”

A new heterotrimetallic sandwich‐like CuII–LaIII–CuII (3d–4f–3d) cluster as a model anticancer drug in interaction with FS‐DNA and BSA and as a new artificial catalyst for catecholase activity

“…[26] The survey on protein-lanthanide complex interaction are investigated because of their potential biological properties. [27,28] Another important area of research is the investigation of different transition metals utilized in the active sites of metalloenzymes [29,30] such as tyrosinase and catecholase, which are important in catalytic reactions. [31] Various mimicked structures with different properties and functions as artificial enzymes have been studied [32] in which metal and ligand are two important factors.…”

“…[ 26 ] The survey on protein–lanthanide complex interaction are investigated because of their potential biological properties. [ 27,28 ]…”