Supramolecular Arrangement and DFT analysis of Zinc(II) Schiff Bases: An Insight towards the Influence of Compartmental Ligands on Binding Interaction with Protein |
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| Authors: | Megha Sen Chowdhury Dr Selcuk Gumus Dr Sanchari Dasgupta Dr Ishani Majumder Dr Abir Bhattacharya Dr Debasis Das Dr Jayanta Mukhopadhyay Dr Debosreeta Bose Dr Saumya Dasgupta Dr Yuksel Akinay Dr Madhumita Mukhopadhyay |
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| Institution: | 1. Department of Chemistry, Amity Institute of Applied Sciences (AIAS), Amity University, 700156 Kolkata, India;2. Van Yuzuncu Yil University, Department of Chemistry, Faculty of Science, 4445065 Van, Turkey;3. Department of Chemistry, University of Calcutta, 92, A. P. C. Road, 700 009 Kolkata, West Bengal, India;4. Department of Physics, The Bhawanipur Education Society College, University of Calcutta, 700020 Kolkata, India;5. Energy Materials & Devices Division, CSIR-Central Glass and Ceramic Research Institute, 700 032 Kolkata, India;6. Van Yuzuncu Yil University, Department of Mining, Engineering Faculty, 4445065 Vancity, Turkey |
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| Abstract: | We report, for the first time, a detailed crystallographic study of the supramolecular arrangement for a set of zinc(II) Schiff base complexes containing the ligand 2,6-bis((E)-((2-(dimethylamino)ethyl)imino)methyl)-4-R-phenol], where R=methyl/tert-butyl/chloro. The supramolecular study acts as a pre-screening tool for selecting the compartmental ligand R of the Schiff base for effective binding with a targeted protein, bovine serum albumin (BSA). The most stable hexagonal arrangement of the complex Zn ? Me] (R=Me) stabilises the ligand with the highest FMO energy gap (ΔE=4.22 eV) and lowest number of conformations during binding with BSA. In contrast, formation of unstable 3D columnar vertebra for Zn ? Cl] (R=Cl) tend to activate the system with lowest FMO gap (3.75 eV) with highest spontaneity factor in molecular docking. Molecular docking analyses reported in terms of 2D LigPlot+ identified site A, a cleft of domains IB, IIIA and IIIB, as the most probable protein binding site of BSA. Arg144, Glu424, Ser428, Ile455 and Lys114 form the most probable interactions irrespective of the type of compartmental ligands R of the Schiff base whereas Arg185, Glu519, His145, Ile522 act as the differentiating residues with ΔG=?7.3 kcal mol?1. |
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| Keywords: | compartmental ligand density functional theory molecular docking Schiff base supramolecular arrangement |
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