Luminescent study on the binding interaction of bioactive imidazole with bovine serum albumin—A static quenching mechanism

Novel bioactive imidazole derivatives were synthesized and characterized by NMR spectra, mass and CHN analysis. The interaction between the imidazole derivative and bovine serum albumin (BSA) was investigated by fluorescence and UV–vis absorption spectroscopy. The fluorescence quenching of BSA by the imidazole derivatives may be due to the formation of imidazole–BSA complex. The fluorescence quenching mechanism of BSA by imidazole was analyzed and the binding constant has been calculated. The binding distance between imidazole and BSA was obtained based on Forester's non-radiation energy transfer (FRET). The effect of some common ions on the binding constant between imidazole and BSA was also examined.

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► The interaction between the imidazole and BSA was investigated spectroscopically.
► There exists a static fluorescence quenching mechanism.
► The conformational change of BSA due to the presence of imidazole.
► The –OH group of Tyr residue for the interaction of BSA with imidazole.
► Static quenching – the donor-to-acceptor distance is <8 nm.