1st International and 10th National Iranian Conference on Bioinformatics
Home Accepted Papers
The Binding Assessment with Human Serum Albumin of Binuclear Ni(II) and Cu(II) Complexes Containing Bidentate 8-Hydroxyquinoline Ligand
Paper ID : 1430-ICB10
Authors:
Mohammad Reza Binaeizadeh1, Ahmad Amiri *2, سودابه شکرالهی1
1university of tehran
2دانشگاه تهران پردیس علوم دانشکده شیمی
Abstract:
The study of human serum albumin (HSA) binding in biophysical and biochemical studies is important since it has a well-known primary structure and it has been associated with the binding of many different categories of small molecules [1]. Metal ions bind to proteins via coordinate bond formation with amino acid side chains. The use of metal complexes allows the formation of targeted protein-bound adducts that show binding via coordination or noncovalent interactions [2]. Herein, two Ni(II) and Cu(II) complexes of the general type [Ni2(Q)6] and [Cu2(Q)4] (Q = 8-hydroxyquinoline) were synthesised and characterised by FT-IR, UV–Vis and 1H-NMR. The optimized structures and frontier orbitals properties were computed using DFT/B3LYP method and LANL2DZ and 6–31G** as basis sets. The electronic structure and spectral characterization of the synthesized complexes have been investigated using the density functional theory (DFT). The interaction of these complexes with protein (HSA) was followed via fluorescence spectroscopy, circular dichroism (CD) and molecular docking simulation. The observation of remarkable quenching in the emission spectrum of HSA upon titration with the complexes with an excellent binding constant (Kb= 93.88 mM-1 for [Ni2(Q)6]) reveals the strong interaction between the complexes and HSA. Furthermore, the Kq values of the fluorescence quenching are greater than 2.0 × 1010 M−1 s−1, establishing the fact that the fluorescence quenching is static. Molecular docking results revealed these complexes bind with HSA, and the binding site was positioned in Sudlow Site II of HSA (subdomain IIB).
Keywords:
8-hydroxyQuinoline; HSA Binding; Molecular Docking; DFT; Circular Dichroism.
Status : Paper Accepted (Poster Presentation)