Synthesis, Characterization, and Drug-Likeness Study of Novel 1-Acetyl-5-(Morpholin-4yl Sulfonyl)Indoline

A novel organic compound, 1-acetyl-5-(morpholin-4yl sulfonyl)indoline was synthesized. The compound was characterized using 1H NMR, 13C NMR, FT-IR, and mass spectroscopy. 1H NMR that displays a chemical shift of multiplet in the δ- 2.49–2.82 confirming indoline CH and NH attachment. 13C NMR spectrum also shows the coupling of the indoline ring with morpholin. The FT-IR spectrum confirms the nitrogen sulfur bond and also the sulfoxide groups. The mass spectra also confirm the formation of the titled compound. DFT studies were conducted using the B3LYP/6–311 ++ G (d, p) as the basis set. DFT studies show HOMO (ev) −7.259 (eV), LUMO (ev) −0.0917 eV, bandgap E 7.24 eV, chemical potential μ 3.6758, global hardness ɳ 3.5814, global softness ζ 0.13950, electrophilicity index (χ) 1.02636 and dipole moment (μ) 2.05271 (Debye). NBO analysis of the compound was studied by Gaussian software, and results indicate that the compound is stabilized by the charge transfer between σ and σ*, π*. Nonlinear property was also studied for the titled compound. In our analysis, we determined that the first-order hyper polarizability of the compound is (4.625 × 10−30 esu). The DFT outcome showed that the molecule can act as a drug, and drug-likeness property of the titled compound was determined using SwissADME. Analysis of the compound showed no violation of the Lipinski rule and no risk in using it as a drug. Docking tests against several proteins downloaded from the rscb.org protein depository were conducted using autodockvina. Cancer proteins and proteins of various pathological bacteria and viruses were docked with the title compound. The compound showed a high docking score (−8 to −9) against proteins with PDB ID 1DMY, 1JD0, 4XMB, and 5NN0. First two proteins belong to carbonic anhydrase, 4XMB is a human Keap protein, and 5NN0 is a huBChE protein. Standard docking procedure such as removing the ligand, water and adding polar bonds were carried out. The stability of the protein–ligand complex was studied using molecular dynamics. RMSF, RMSD, and Sasa analyses were studied in the molecular dynamics study, and Gromacs software was utilized for this purpose. Of the four protein–ligand complexes, 5NN0 showed the highest stability with RMSD variation less than 0.5. The titled compound has yet to be tested in vitro and in vivo.