Experimental, insilico, DFT studies of novel compound 2-{2-[(3,4-dimethoxyphenyl)methylidene]hydrazinecarbonothioyl}-N-methyl-N- phenylhydrazine-1-carbothioamide

Abstract

In the current investigation, we have obtained single crystals 2-{2-[(3,4-dimethoxyphenyl)methylidene]hydrazinecarbonothioyl}-N-methyl-N-phenylhydrazine-1-carbothioamide (H2L) by refluxing 3,4 dimethoxybenzaldehyde and N(4)- methyl-N(4)-phenyl thiosemicarbazide. Here we discuss the experimental as well as theoretical studies of the selected molecule. Computational studies were made by Gaussian 09 program. X-ray refinement data of the molecule is used for geometry optimization process using DFT (B3LYP) method with the 6–31 + G (d,p) basis sets. The optimised molecular structure, MEP, NBO, HOMO-LUMO analysis, and NLO effects of 2-{2-[(3,4-dimethoxyphenyl)methylidene]hydrazinecarbonothioyl}-N-methyl-N-phenylhydrazine-1-carbothioamide have been communicated in this paper. NBO analysis gave insight into the strongly delocalized structure, responsible for the nonlinearity and hence the stability of the molecule. H2L obeys Lipinski’s rule, and further in silico assessment of oral bioavailability, ADME, drug-likeness, and medicinal chemistry friendliness proposes that this molecule is a promising candidate for the cancer drug discovery process. Simultaneously, molecular docking of the compound into the 3D crystal structure of ribonucleotide reductase M−2 subunit (PDB ID: 2UW2) and Histone deacetylase 8 (PDB ID 1 T69) have been performed using GLIDE Dock Program. The study has shown that the ligand could be a potential inhibitor for the ribonucleotide reductase M−2 subunit protein.

Keywords

• Single crystal XRD
• NBO
• NLO
• ADME
• Molecular Docking
• Ribonucleotide reductase