Evaluation of the Binding Affinities of Mixed Ligands Metal (II) Complexes of Quercetin Sulphonic Acids on Breast Cancer Cells Using Molecular Docking.

Abstract

sulphonic acids on a protein macromolecule from Breast Cancer cells using molecular docking. The protein macromolecule with code: 1OQA, was downloaded from the protein data bank and prepared using the Discovery Studio software, the mixed-ligands metal (II) complexes of quercetin-5-sulphonic and quercetin-8-sulphonic acids were drawn using Chemsketch software and afterwards converted to a structure data format (sdf) with the help of Open Babel software. The co-ligands used in this study included Benzoic, Citric, Isophthalic, Oxalic, Salicylic, Succinic, Terephthalic acids and Imidazole. The docking was performed with PyRx software, and visualized with Discovery Studio. The results indicate that apart from the nature of the binding sites of the breast cancer cell protein 1OQA, the position of the sulphonic substituent on the quercetin ring, the type of metal ion used in the coordination, and the nature of the co-ligand all affected the binding affinities of the complexes. Generally, the observed enhanced binding affinities of the complexes seem to be more pronounced when Benzoic, Isophthalic acids and Fe²⁺, Mn²⁺ ions are involved in the structures. Also, the co-ligand with aromatic ring shows enhanced affinity compared to aliphatic co-ligands with several variations.