Studies of the interaction of bovine serum albumin with pyrimidine-annulated spiro-dihydrofuran and
1Department of Biochemistry and Biophysics, University of Kalyani, Kalyani 741235, West Bengal, India
2School of Sciences, NetajiSubhas Open University, Kolkata 700064, India
3Department of Chemistry, University of Kalyani, Kalyani 741235, West Bengal, India
Adv. Mater. Lett., 2015, 6 (11), pp 1018-1024
Publication Date (Web): Oct 26, 2015
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The interaction between pyrimidine-annulated spiro-dihydrofuran (PSDF) with bovine serum albumin (BSA) was investigated following spectroscopic studies. The results indicate that dynamic quenching contributes to the fluorescence quenching of BSA by PSDF. The binding constant (K) and the number of binding sites (n) were calculated from the recorded spectra. Based on the Förster’s non-radiative energy transfer theory, the average binding distance between BSA and PSDF was estimated. The synchronous fluorescence spectra and circular dichroism indicate that the conformation of BSA has been subjected to alteration in presence of PSDF. The thermodynamic parameters namely ΔH, ΔG, ΔS were calculated at different temperatures (20 oC, 30 oC, and 40 oC) and the results indicated van der Waals force and hydrogen bonding were predominantly present. The compound PSDF also found to exhibit antifungal activity against Aspergillus sp. In addition, the results obtained from molecular modeling calculation vividly elucidate the binding mode and the binding sites and results were not well in agreement with the experimental observations.
PSDF, BSA, UV-Vis spectroscopy, quenching, docking.