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Updated: May 29, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
Binding interaction of bioactive imidazole with bovine serum albumin--a mechanistic investigation
Jayaraman Jayabharathi1, Venugopal Thanikachalam, Kumar Brindha Devi
1Department of Chemistry, Annamalai University, Annamalainagar, Tamilnadu, India. jtchalam2005@yahoo.co.in
Abstract:
A novel Y-shaped imidazole derivative 4-((E)-2-(4,5-diphenyl-1-p-tolyl-1H-imidazol-2-yl)vinyl)phenol has been synthesized and characterised by IR, UV-vis, mass and NMR spectral techniques. The mutual interaction of this imidazole derivative (DPTIV) with bovine serum albumin (BSA) was investigated using photoluminescent studies. The fluorescence quenching mechanism of BSA by DPTIV was analyzed and the binding constant has been calculated. The binding distance between DPTIV and BSA was obtained based on the theory of Forester's non-radiation energy transfer. The effect of some common ions on the binding constant between DPTIV and BSA was also examined.
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