Binding interaction of 1-(4-methybenzyl)-2-p-tolyl-1H-benzo[d]imidazole with bovine serum albumin

A promising benzimidazole derivative 1-(4-methybenzyl)-2-p-tolyl-1H-benzo[d]imidazole (MBTBI) has been synthesized and characterized by single crystal XRD, NMR, mass and IR spectral techniques. The mutual interaction of this benzimidazole derivative (MBTBI) with bovine serum albumin (BSA) was investigated using solution spectral studies. The fluorescence quenching mechanism of BSA by MBTBI was analyzed and the binding constant has been calculated. The binding distance between these two was obtained based on the theory of Forester's non-radiation energy transfer (FRET). The effect of some common ions on the binding constant was also examined.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The interactions between dfppip and BSA were investigated by fluorescence quenching. ► Quenching mechanism mainly arise from the formation of BSA–MBTBI complex. ► The D → A distance is <8 nm indicates that the energy transfer from BSA to MBTBI. ► Synchronous fluorescence spectra to exploit the structural change of BSA. ► The effect of other ions on the binding constants between MBTBI and BSA.