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| Study on Interaction between Alliin and Bovine and Hunman Serum Albumin with Spectrometry |
| MA Xue-hong1, SONG Bai-ling2, XIAO Wen-jun2, GENG Jing2, LI Xin-xia1*, CHEN Jian3 |
1. Central Laboratory, Xinjiang Medical University, Urumqi 830011, China
2. College of Pharmacy, Xinjiang Medical University, Urumqi 830011, China
3. Xinjiang Ailexin Pharmacy Limited Company, Urumqi 830000, China |
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Abstract The interaction between alliin and bovine serum albumin(BSA) and human serum albumin(HSA) was studied under a pH7.4 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 9.81×102 L·mol-1 at 298 K and 6.15×102 L·mol-1 at 310 K. The binding constant obtained of alliin and HSA was 2.21×102 L·mol-1 at 298 K and 6.84×102 L·mol-1 at 310 K. The thermodynamic parameters, ΔH calculated by using Gibbs-Helmholtz Equation of the reaction of alliin and BSA is -29.9 kJ·mol-1 and ΔS is 43.0 J·mol-1·K-1 and ΔG is -17.1 kJ·mol-1 at 298 K. ΔH of the reaction of alliin and HSA is 72.3 kJ·mol-1 and ΔS is 288 J·mol-1·K-1 and ΔG is -13.4 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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Received: 2015-10-21
Accepted: 2016-02-19
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Corresponding Authors:
LI Xin-xia
E-mail: lxx6668@163.com
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