Molecular Docking and Molecular Dynamic Studies, Synthesis, Characterisation of Thiazolidine-4-One Derivatives

Abstract

Background: Antibacterial, antifungal, anticancer, antitubercular, anti-HIV, analgesic, anti-inflammatory, and ulcerogenic activities have all been documented for thiazolidine derivatives. Molecular docking has become a crucial step in the drug discovery process, with the goal of predicting the binding mechanism and affinity of the protein-ligand complex. AutoDock is a popular non-commercial docking tool that successfully docks ligands to their target proteins (accurate and computationally fast). The Discovery Studio Visualizer is a free viewer that may be used to open data produced by other Discovery Studio tools.
 Aim: The main aim of this study is:
 
 To study the molecular docking and molecular dynamic studies of the different thiazolidine derivatives.
 To synthesise the compound based on the results produced in the molecular dynamics and molecular studies.
 To Characterise the synthesised compounds using FTIR, 1H NMR, 13C NMR and Mass Spectral studies.
 
 Procedure: In two phases, a new series of Thiazolidine-4-one derivatives was created. The production of Schiff base is the first step, followed by the condensation of Schiff base with Chloro acetyl chloride and subsequent cyclisation steps. FTIR, 1H-NMR, 13C-NMR, and Mass Spectroscopy were used to characterise the chemical structures of the produced compounds.
 1BVR protein that was taken from the protein database website
 The structures were drawn using Chem draw Ultra 8.0 and Biovia draw 2018. Using the Smiles Online Translator, it was stored in Mol format and then converted to PDB format. The Cygwin toolings were used to log all of the files.
 Conclusion: The conformation was computed using a ranking system. This indicates whether the molecule has strong ligand binding energy, hydrogen bonding, and hydrophobic interaction with the receptor. According to the findings, thiazolidine-4-one derivatives have antitubercular efficacy when used in conjunction with the Enoyl-acyl carrier protein (enoyl-ACP) reductase enzyme.
 For the docking analysis it indicates if the compound has strong ligand binding energy, hydrogen bonding, and hydrophobic binding with the receptor shows good activity. Using Auto dock 4.2 it was found out that among the above 20 compounds (including the control compound), C2, C5, C6, C8, C11. C13, C15 and C17 directly bind with the functional domain (Casein kinase II phosphorylation site) of the amino acid (252 to 255). The above compounds bind at the 252nd position of the Chain C, where Alanine is present (The target protein, 1BVR () contains ABCDEF chains).