Effect of N-, S- and O-Substitutions of Isophthalic Acid Derivatives on their Binding Properties: An <i>In-Silico</i> Approach

The fuel industry, particularly the petroleum industry, uses organic compounds for different reasons to improve fuels to obtain the desired products. This review studies the binding of organic molecules with a protein. Binding studies of the N-, S- and O-substitutions of Isophthalic acid derivatives with COVID-19 protein were examined by molecular docking approach. In investigations using molecular docking, the ligand is attached to the protein's binding pocket in various ways, yielding crucial information regarding the binding site and method. Molecular docking experiments were performed to comprehend how Isophthalic acid derivatives and COVID-19 protein interactions take place. The docking research was conducted using Autodock 4.2.5. Auto Dock forecasts the binding conformations of flexible ligands to bio-macromolecular targets via the Lamarckian genetic technique. The technique involved adding Kollman charges and polar hydrogen to the ligand and protein molecules to produce the PDBQT files and combining non-polar bonds to produce molecular probes. To perform conformational search and docking simulation, the Lamarckian Genetic Algorithm (LGA) was chosen. PyMOL was used as a visualising tool. It was found that the principal binding forces in the interaction between Isophthalic acid derivatives and selected proteins were hydrophobic interactions and hydrogen bonding. The molecular probe's ideal form revealed the affinity as a release of freebinding energy. The current research report aims to highlight the approachable nature of derivatives of isophthalic acid and paves the way for focused biological interactions.