Docking investigation and binding interaction of benzimidazole derivative with bovine serum albumin
1H NMR, 13C NMR and Mass spectral analysis have been made for 1-(4-fluorobenzyl)-2-(4-fluorophenyl)-1H-benzo[d]imidazole (FBFPB). The mutual interaction of FBFPB with bovine serum albumin (BSA) was investigated using absorption, fluorescence and synchronous fluorescence spectral studies. The binding distance has been determined based on the theory of Forester’s non-radiation energy transfer (FRET). The calculated quenching constants (Ksv) were 2.84 × 104, 2.55 × 104 and 2.37 × 104 at 301, 310 and 318 K respectively. The Stern–Volmer quenching constant (Ksv), binding site number (n), apparent binding constant (KA) and corresponding thermodynamic parameters (ΔG, ΔH and ΔS) were calculated. The interaction between FBFPB and BSA have discussed by molecular docking technique.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The interactions between FBFPB and BSA were investigated. ► Quenching mechanism mainly arise from the formation of BSA–FBFPB complex. ► The D → A distance indicates that the energy transfer from BSA to FBFPB. ► Synchronous fluorescence spectra to exploit the structural change of BSA. ► Molecular docking technique discussed.
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 117, 5 December 2012, Pages 27–32