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林产化学与工业

林产化学与工业 ›› 2011, Vol. 31 ›› Issue (5): 60-64.

• 研究报告 • 上一篇    下一篇

茄尼醇与牛血清白蛋白相互作用的研究

高义霞, 周向军, 王风霞, 张花   

  1. 天水师范学院 生命科学与化学学院, 甘肃 天水 741001
  • 收稿日期:2011-01-24 修回日期:1900-01-01 出版日期:2011-10-30 发布日期:2011-10-30

Interaction between Solanesol and Bovine Serum Albumin

GAO Yi-xia, ZHOU Xiang-jun, WANG Feng-xia, ZHANG Hua   

  1. College of life science and chemistry, Tianshui Normal University, Tianshui 741001, China
  • Received:2011-01-24 Revised:1900-01-01 Online:2011-10-30 Published:2011-10-30

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摘要： 在模拟人体生理条件下,研究了茄尼醇与牛血清白蛋白(BSA)的相互作用。采用荧光及紫外吸收法测定了茄尼醇对牛血清白蛋白的猝灭常数、结合常数、结合位点、结合距离及热力学参数。结果表明,当温度为25和 37 ℃ 时,茄尼醇对牛血清白蛋白的猝灭常数分别为1.76×107和2.7×107 mol/L,结合常数(KA)分别为1.54×106和1.9×106 mol/L,结合位点数分别为1.09和1.50,结合距离(r)0 nm,热力学参数均为ΔG<0,ΔH>0,ΔS>0。因此,茄尼醇对牛血清白蛋白有较强的猝灭作用,猝灭方式为静态猝灭,它们之间的结合以疏水作用为主,且计算出茄尼醇插入BSA内部并与212位色氨酸结合。

关键词: 荧光光谱法, 紫外吸收法, 茄尼醇, 牛血清白蛋白, 荧光猝灭

Abstract: Under simulated physiological conditions, the interaction between solanesol and bovine serum albumin(BSA) was investigated. The quenching constant, binding constant, the number of binding site and binding distance were determined by fluorescence spectroscopy and ultraviolet absorption spectroscopy. They were 1.76×107 and 2.7×107 mol/L, 1.54×106 and 1.9×106 mol/L, 1.09 and 1.50, and r=0 nm at 25 ℃ and 37 ℃, respectively. Thermodynamic parameters were ΔG<0,ΔH>0,ΔS>0. So the fluorescence of bovine serum albumin was strongly quenched by solanesol in the static quenching style. Thermodynamics analysis demonstrated that the hydrophobic interaction force played a main role in the binding of solanesol with bovine serum albumin and solanesol was inserted into bovine serum albumin at tryptophan 212.

Key words: fluorescence spectroscopy, UV spectroscopy, solanesol, bovine serum albumin, fluorescence quenching

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