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Updated: Apr 11, 2026
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Synthesis, structure, protein binding of Cu(II) complexes with a tridentate NNO Schiff-base ligand
Mei Li1, ShuJuan Huang1, Cheng Ye1
1Key Laboratory of Jiangxi University for Functional Material Chemistry, College of Chemistry & Chemical Engineering, Gannan Normal University, Ganzhou, Jiangxi, China.
Abstract:
Four new Cu(II) complexes (1, 2, 3 and 4) in the presence of different anions (Cl(-), Br(-), I(-) and ClO4(-)) have been prepared by tridentate NNN Schiff-base ligand (N,N-dimethyl-N'-[phenyl(2-pyridyl)methylene]ethane-1,2-diamine) and well characterized by single-crystal X-ray diffraction, elemental analysis, IR and UV-Vis spectroscopy. The interactions of complexes 1-4 with human serum albumin (HSA) have been investigated in Tris-HCl buffer solution at pH 7.4 by spectroscopic methods and a molecular docking technique. Experimental results proved that the four complexes quench the fluorescence of HSA through a static quenching mechanism. Thermodynamic parameters were calculated from Van't Hoff equation. The distance r between the donor (HSA) and acceptor (complexes 1-4) has been obtained by means of Förester resonance energy transfer (FRET). Molecular docking results indicated that the main active binding sites for complexes 1, 2 and 4 are site III in subdomain IB and for complex 3 is site II in subdomain III A. The combination of molecular docking results and fluorescence experimental results indicate that the interaction between 1-4 and HSA are dominated by hydrophobic forces as well as hydrogen bonds.
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