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Study on the Interaction between Florasulam and Bovine Serum Albumin

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Abstract

In this paper, the interaction between florasulam (FU, 2′,6′,8-trifluoro-5-methoxy [Kragh-Hansen U, Molecular aspects of ligand binding to serum albumin. Pharmacol Rev 33(1):17–53 1981; Carter DC and Ho JX, Structure of serum albumin. Adv Protein Chem 45:153–203 1994; He XM, and Carter DC, Atomic structure and chemistry of human serum albumin. Nature 358(6383):209–215 1992] triazolo [1,5-c]pyrimidine-2-sulfonanilide) and bovine serum albumin (BSA) was investigated by fluorescence, ultraviolet absorption (UV) and Far-UV circular dichroism (CD) spectrometries. A strong fluorescence quenching was observed and the quenching mechanism was considered as static quenching. The binding constant of FU with BSA at 299 and 309 K were obtained as 1.5 × 104 and 7.1 × 103 l mol−1, respectively. There was one binding site between FU and BSA. The thermodynamic parameters enthalpy change (ΔH) and entropy change (ΔS) were calculated as −57.89 kJ mol−1 and −113.6 J mol−1 K−1, respectively, which indicated that the acting force between FU and BSA was mainly hydrogen bond and Van der Waals force. According to the Förster non-radiation energy transfer theory, the average binding distance between donor (BSA) and acceptor (FU) was obtained (r = 1.59 nm). The investigations of the UV/Vis and CD spectra of the system showed that the conformation of BSA was changed in presence of FU.

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Acknowledgements

This work is supported by the Natural Science Foundations of China (20575035) and Shandong Province (Y2003B02).

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Correspondence to Xia Wu or Jinghe Yang.

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Ran, D., Wu, X., Zheng, J. et al. Study on the Interaction between Florasulam and Bovine Serum Albumin. J Fluoresc 17, 721–726 (2007). https://doi.org/10.1007/s10895-007-0226-9

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