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

Sensors International

B.R. Jali¹  Suban K. Sahoo²  Anil K. Verma³  M. Mohanty⁴  R. Dinda⁴  P. Mohanty⁵  R. Behura⁵  S. Behera⁵ 

[1] Corresponding author.;Department of Applied Chemistry, S.V. National Institute of Technology, Surat, 395007, India;Department of Biosciences and Biotechnology, Sikkim University, Gangtok, 737102, India;Department of Chemistry, National Institute of Technology, Rourkela, 769008, Odisha, India;Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur, 768018, Odisha, India;

关键词: Schiff base;    Protein-ligand interaction;    Molecular docking;    Cytotoxicity;    Fluorescence;    Binding constant;   

DOI  :  

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown