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Binding interaction of phosphorus heterocycles with bovine serum albumin:A biochemical study

Journal of Pharmaceutical Analysis 2017年第1期7卷 19-26页

作者： Swarup Roy Raj Kumar Nandi Sintu Ganai K.C. Majumdar Tapan K. Das Department of Biochemistry and Biophysics University of Kalyani Kalyani 741235 West Bengal India Department of Chemistry University of Kalyani Kalyani 741235 West Bengal India

Interaction between bovine serum albumin(bsa) and phosphorus heterocycles(phs) was studied using multispectroscopic techniques. The results indicated the high binding affinity of phs to bsa as it quenches the intrinsic fluorescence of bsa. The experimental data suggested the fluorescence quenching mechanism between phs and bsa as a dynamic quenching. From the UV–vis studies, the apparent association constant(K_(app)) was found to be 9.25×10~2, 1.27×10~4and 9.01×10~2L/mol for the interaction of bsa with PH-1, PH-2 and PH-3,respectively. According to the F?rster's non-radiation energy transfer(FRET) theory, the binding distances between bsa and phs were calculated. The binding distances(r) of PH-1, PH-2 and PH-3 were found to be2.86, 3.03, and 5.12 nm, respectively, indicating energy transfer occurs between bsa and phs. The binding constants of the phs obtained from the fluorescence quenching data were found to be decreased with increase of temperature. The negative values of the thermodynamic parameters ΔH, ΔS and ΔG at different temperatures revealed that the binding process is spontaneous; hydrogen bonds and van der Waals interaction were the main force to stabilize the complex. The microenvironment of the protein-binding site was studied by synchronous fluorescence and circular dichroism(CD) techniques and data indicated that the conformation of bsa changed in the presence of phs. Finally, we studied the bsa-phs docking using Auto Dock and results suggest that phs is located in the cleft between the domains of bsa.

关键词： bsa Spectroscopy Phosphorus heterocycles bsa-phs docking

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