Sen Chowdhury, Megha and Gumus, Selcuk and Dasgupta, Sanchari and Majumder, Ishani and Bhattacharya, Abir and Das, Debasis and Mukhopadhyay, Jayanta and Bose, Debosreeta and Dasgupta, Saumya and Akinay, Yuksel and Mukhopadhyay, Madhumita (2022) Supramolecular Arrangement and DFT analysis of Zinc(II) Schiff Bases: An Insight towards the Influence of Compartmental Ligands on Binding Interaction with Protein. ChemistryOpen, 11 (6). Art No-e202200033. ISSN 2191-1363

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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 (Delta E=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 Delta G=-7.3 kcal mol(-1).

Item Type:	Article
Subjects:	Crystal Chemistry, Thermodynamics, Phase Equilibria
Divisions:	UNSPECIFIED
Depositing User:	Bidhan Chaudhuri
Date Deposited:	21 Sep 2023 07:12
Last Modified:	21 Sep 2023 07:12
URI:	http://cgcri.csircentral.net/id/eprint/5523

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