Abstract
Three new p-halogenated cinnamic amides (p-CA) have been synthesized and the interactions between p-CA and bovine serum albumin (BSA) in pH 7.4 tris–HCl buffer solution have been investigated by fluorescence and ultraviolet spectroscopies. Fluorescence spectra revealed that the quenching was a static quenching process at low p-CA concentrations and a combined quenching (static and dynamic) process at higher p-CA concentrations. The Stern–Volmer quenching constants (K SV), the binding constants (K A), the number of binding sites (n), and the thermodynamic parameters (ΔG, ΔH, and ΔS) have been calculated at 298, 303, and 308 K. According to Föster’s non-radiative energy transfer theory, the binding distances between p-CA and BSA are determined and the resonance energy transfer in p-CA and BSA has high possibility. The investigation of synchronous fluorescence spectra suggested that the binding of p-CA to BSA changed the microenvironment around the tyrosine residues. In addition, three halogens have different effects on binding interactions when they are introduced to the cinnamic amides.
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Acknowledgments
This work was financially supported by the Natural Science Foundation of China (21362001), Natural Science Foundation of Guangxi Province (2013GXNSFDA019005), Youth Foundation of Guangxi Botanical Garden of Medicinal Plant project (Grant No. guiyaoji201108), and the Guangxi University Foundation of Training Undergraduate Students’ Experimental Skills and Innovational Abilities (SYJN20120306).
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Wei, J., He, Y., Bei, G. et al. Fluorometric Investigation of the Interaction of (2E)-3-(4′-Halophenyl)-N-{4′′-[(5′′′,6′′′-dimethoxypyrimidin-4′′′-yl)sulfamoyl]phenyl}prop-2-enamides with Bovine Serum Albumin. Proc. Natl. Acad. Sci., India, Sect. A Phys. Sci. 84, 505–516 (2014). https://doi.org/10.1007/s40010-014-0165-1
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DOI: https://doi.org/10.1007/s40010-014-0165-1