Binding Interaction of Organofluorine-Serum Albumin: A Comparative Ligand-Detected 19 F NMR Analysis

The Journal of Physical Chemistry. B
Bhawna Chaubey, Samanwita Pal

Abstract

In the present study, we attempt to characterize fluorinated ligand-serum albumin interaction in solution by a set of one-dimensional 19F ligand-based experiments. In this regard, a model system diflunisal (DFL)-human serum albumin (HSA) has been chosen to benchmark the utility of 19F relaxation and diffusion-based experiments in deciphering ligand-protein interactions. Further, we extend the application of a similar set of 19F experiments to unravel the molecular interaction in an unexplored system of 2,6-difluorobenzoic acid (DFBA)-bovine serum albumin (BSA). Interaction analysis of DFBA-SA is of particular interest because DFBA is not only a stable metabolite of a number of pesticides but also used as the starting reagent of many fluorinated drugs. Observation of 19F-1H & 1H-1H saturation transfer difference effects confirmed binding of the ligands to SA. Further, these ligand-protein complexes were probed in terms of the dissociation constant ( KD), number of binding sites ( n), bound fraction of the ligand ( Pb), the complex lifetime (τres), and exchange rate ( Kex). Although Carr-Purcell-Meiboom-Gill (CPMG)-based transverse relaxation and diffusion analysis quantified the former three quantities, the latter two were deter...Continue Reading

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Citations

Jan 6, 2021·Environmental Science and Pollution Research International·Bhawna ChaubeySamanwita Pal

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