Spectroscopy and Spectral Analysis, Volume. 37, Issue 6, 1826(2017)
Study on Interaction between Alliin and Bovine and Hunman Serum Albumin with Spectrometry
The interaction between alliin and bovine serum albumin(BSA) and human serum albumin(HSA) was studied under a pH74 Tris-HCl buffer system with multiple spectroscopic techniques.The study took 280 nm as the excitation wavelength to scan the range of 300~500 nm of fluorescence emission spectrum by using fluorescence spectrophotometer while setting wavelength differential as Δλ=15 nm and Δλ=60 nm to scan synchronous fluorescence spectra. The fluorescence quenching data were analyzed by applying Stern-Volmer equation and Line weaver-Burk equation. It is shown that Alliin was effective in quenching BSA and HSA fluorescence. The binding constant obtained of alliin and BSA was 981×102 L·mol-1 at 298 K and 615×102 L·mol-1 at 310 K. The binding constant obtained of alliin and HSA was 221×102 L·mol-1 at 298 K and 684×102 L·mol-1 at 310 K. The thermodynamic parameters, ΔH calculated by using Gibbs-Helmholtz Equation of the reaction of alliin and BSA is -299 kJ·mol-1 and ΔS is 430 J·mol-1·K-1 and ΔG is -171 kJ·mol-1 at 298 K. ΔH of the reaction of alliin and HSA is 723 kJ·mol-1 and ΔS is 288 J·mol-1·K-1 and ΔG is -134 kJ·mol-1 at 298 K. The main types of binding force of Alliin-BSA were hydrophobic interaction and the sorts of binding force of Alliin-HSA were electrostatic action. The results of synchronous fluorescence spectra showed that alliin has main effects on Tyr of BSA and both Tyr and Trp of HSA. The experimental results have provided the certain theory basis of the mechanism of interaction between alliin and biological small molecules.
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MA Xue-hong, SONG Bai-ling, XIAO Wen-jun, GENG Jing, LI Xin-xia, CHEN Jian. Study on Interaction between Alliin and Bovine and Hunman Serum Albumin with Spectrometry[J]. Spectroscopy and Spectral Analysis, 2017, 37(6): 1826
Received: Oct. 21, 2015
Accepted: --
Published Online: Jul. 10, 2017
The Author Email: Xue-hong MA (mxh6867@163com)