Multi-spectroscopic Studies of the Interaction of Linalool with Bovine Serum Albumin
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Abstract:
The mechanisms of the interaction between linalool and bovine serum albumin (BSA) and the effect of linalool on the BSA conformation under simulated physiological conditions were investigated by fluorescence, ultraviolet-visible (UV-Vis) absorption, Fourier transform infrared (FT-IR)and Raman spectroscopies. The obtained results indicate that linalool can quench the intrinsic fluorescence of BSA regularly, and that the mechanism underlying was the static quenching via the was the formation of BSA-linalool complexes. The binding constants and the numbers of binding sites at different temperatures were calculated. According to the thermodynamic parameters, the interaction between linalool and BSA is a spontaneous process with a decrease in the Gibbs free energy value. The main forces in this process are hydrogen bonding and van der Waals forces. The binding distance between linalool and BSA was calculated according to the Forster’s theory of non-radioactive energy transfer. Furthermore, the UV-Vis, synchronous fluorescence, FT-IR and Raman spectra demonstrated that the conformation of BSA changes after its interaction with linalool, which includes a decrease in α-helical content and a more hydrophobic microenvironment of tryptophan and tyrosine residues.
