摘要
利用荧光光谱、CD和FTIR技术研究了模拟生理条件下厚朴酚与人血清白蛋白的相互作用,计算了反应的结合常数、结合位点数和热力学参数。厚朴酚在人血清白蛋白上的结合位置与色氨酸残基间的距离为2.34 nm。分子模型研究表明,厚朴酚与HSA在亚结构域IIA结合,二者间的作用力主要为疏水作用。CD结果表明,厚朴酚与HSA的键合使HSA中α-螺旋结构含量从46.6%降到39.9%。
A combination of intrinsic fluorescence, circular dichroism （CD） and fourier transform infrared （FTIR） technique was used to investigate the binding between magnolol and human serum albumin （HSA） under simulated physiological conditions. The binding parameters （K） and the binding sites （n） at 296 K, 310 K and 318 K were obtained, which are 2. 256 × 10^5 L/mol, 2. 072 × 10^5 L/mol and 0.67, 0.62, 0.57, respectively. The enthalpy change （AH） and the entropy change （AS） were calculated to be -4.57 kJ/mol and 87.03 J/mol -K respectively. Which indicated that hydrophobic forces played major role in the interaction of magnolol and HSA and were consistent with the result of molecule modeing study. Furthermore, The results of molecular modeling study indicate that magnolol and HSA was obtained （2.34 nm） based on the theory of Foerster energy transfer. The result of CD indicated that the α-helix content of HSA decreased from 46.6% to 39.9% after magnolol bound to HSA.
出处
《分析化学》
SCIE
EI
CAS
CSCD
北大核心
2006年第4期557-560,共4页
Chinese Journal of Analytical Chemistry
基金
四川省教育厅重点项目(No.2004A186)
绵阳师范学院博士基金启动项目
