Supramolecular Arrangement and DFT analysis of Zinc(II) Schiff Bases: An Insight towards the Influence of Compartmental Ligands on Binding Interaction with Protein

ChemistryOpen

Dr. Debosreeta Bose¹  Dr. Saumya Dasgupta¹  Megha Sen Chowdhury¹  Dr. Madhumita Mukhopadhyay¹  Dr. Ishani Majumder²  Dr. Debasis Das²  Dr. Sanchari Dasgupta²  Dr. Abir Bhattacharya³  Dr. Jayanta Mukhopadhyay⁴  Dr. Selcuk Gumus⁵  Dr. Yuksel Akinay⁶ 

[1] Department of Chemistry Amity Institute of Applied Sciences (AIAS) Amity University 700156 Kolkata India;Department of Chemistry University of Calcutta 92, A. P. C. Road 700 009 Kolkata West Bengal India;Department of Physics The Bhawanipur Education Society College University of Calcutta 700020 Kolkata India;Energy Materials & Devices Division CSIR-Central Glass and Ceramic Research Institute 700 032 Kolkata India;Van Yuzuncu Yil University Department of Chemistry Faculty of Science 4445065 Van Turkey;Van Yuzuncu Yil University Department of Mining Engineering Faculty 4445065 Vancity Turkey;

关键词: compartmental ligand;    density functional theory;    molecular docking;    Schiff base;    supramolecular arrangement;   

DOI  :  10.1002/open.202200033

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown