Abstract
Three independent techniques have been used to investigate the interaction between bovine serum albumin (BSA) and xanthoxylin (XT). UV-Vis absorption spectroscopy measurements showed that there is a XT-BSA complex formed with an overall binding constant of K=1.01×105 L⋅mol−1. Spectroscopic techniques including synchronous fluorescence and Fourier transform infrared (FT-IR) were used to assess the structural effects of XT binding on BSA. The FT-IR experiments showed that there is a decrease of the amount of α-helix from 50.2 to 48.1% and an increase of the β-sheet from 32.9 to 36.9% in the XT-BSA complex. In addition, XT binds to site I of the protein with a distance of 2.07 nm between tryptophan residues and XT.
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Wen, MG., Zhang, XB., Tian, JN. et al. Binding Interaction of Xanthoxylin with Bovine Serum Albumin. J Solution Chem 38, 391–401 (2009). https://doi.org/10.1007/s10953-009-9385-4
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DOI: https://doi.org/10.1007/s10953-009-9385-4