Spectroscopic, cytotoxicity and molecular docking studies on the interaction between 2,4-dinitrophenylhydrazine derived Schiff bases with bovine serum albumin

Abstract

The 2,4-dinitrophenylhydrazine derived Schiff bases (E)-1-(2,4-dinitrophenyl)-2-(n-nitrobenzylidene)hydrazine (where, n = 2, L1; n = 3, L2 and n = 4, L3) were synthesized and characterized by FTIR, 1H NMR and mass spectra. The interaction of the ligands (L1-L3) with the protein BSA was investigated by fluorescence spectroscopy and molecular docking methods. The fluorescence titration experiments of BSA resulted in fluorescence quenching with the incremental addition of the ligands (L1-L3). The fluorescence quenching is static in nature, and the estimated Stern-Volmer constants of the ligands with BSA followed the order of L1 ≈ L3 > L2. The modes of binding of the ligands with BSA were explored by molecular docking analysis. In addition, the cytotoxicity of the ligands was examined in live HeLa and HT-29 cells. The IC50 values were found in the range 13 μM–243 μM.

Keywords

• Schiff base
• Protein-ligand interaction
• Molecular docking
• Cytotoxicity
• Fluorescence
• Binding constant