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GAO Yi-xia2.7×107 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。
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 ΔG0,ΔH0,ΔS0.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.
出处
《林产化学与工业》
EI
CAS
CSCD
北大核心
2011年第5期60-64,共5页
Chemistry and Industry of Forest Products
基金
陇南地区灾后住宅重建与特色农产品快速生产技术集成及示范项目(2008BAK51B05)
国家自然科学基金资助项目(50773064)
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
fluorescence spectroscopy
UV spectroscopy
solanesol
bovine serum albumin
fluorescence quenching
