Citation: JIANG Tao, MA Liang, ZHANG Yu-Hao, WANG Jia-Man. Fluorescence Spectroscopic Study of Interaction between Aflatoxin B1 and Human Serum Albumin[J]. Chinese Journal of Analytical Chemistry, ;2016, 44(1): 54-60. doi: 10.11895/j.issn.0253-3820.150657 shu

Fluorescence Spectroscopic Study of Interaction between Aflatoxin B1 and Human Serum Albumin

1.
College of Food Science, Southwest University, Chongqing 400715, China

Corresponding author: MA Liang,
Received Date: 19 August 2015
Available Online: 22 October 2015
Fund Project: 本文系国家重点基础研究发展计划(973计划)项目(No.2013CB127803) (973计划)项目(No.2013CB127803)国家自然科学基金项目(No.31301476) (No.31301476)中央高校基本科研业务费专项资金项目(No.2362014xk11) (No.2362014xk11)

Aflatoxin B1 (AFB₁) is the most powerful cancer-causing mycotoxins, which is serious harmful to human and animal health. Human serum albumin has important physiological functions in the binding or transporting endogenous and exogenous ligands aspects. It's great significance in molecular toxicology of researching AFB₁ and human serum albumin interaction mechanism. The interaction between AFB₁ and human serum albumin (HSA) was investigated by fluorescence spectroscopy, circular dichroism and 3D fluorescence spectroscopy under the simulative physiological conditions (pH=7.4, Ionic strength 0.1 mol/L). Results showed that the main quenching mechanism between AFB₁ and HSA was a static quenching process. At four different temperatures (298, 303, 308 and 313 K), all the magnitude binding constants (K) were 104 and the number of binding sites (n) in the binary system was approximate to 1. According to Van't Hoff equation, the negative enthalpy change (ΔH^θ) and postive entropy change (ΔS^θ) values indicated that hydrophobic interaction and hydrogen bonding were the mainly interaction and force in the binding process. The binding distance (r) between the AFB₁ and HSA was calculated to be 3.31 nm based on the theory of F rster's non-radiation energy transfer. The site marker displacement experiments suggested the location of AFB₁ binding to HSA was site I, closely Trp-214. The 3D florescence revealed that the microenvironment of amino acid residues and the conformation of HSA were changed during the binding reaction. CD spectra revealed that the conformations of HSA were changed during the binding reaction with increasing in α-helix.
- Aflatoxin B1,
- Human serum albumin,
- Binding interaction,
- Spectroscopy
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沈阳化工大学材料科学与工程学院沈阳 110142