柚皮苷与人血清白蛋白相互作用的研究  

Study on the interaction of naringin with human serum albumin

作　　者：何丽君[1] 霍彩霞[1] 李生英[1] 姚小军[2] 杨彩玲[1] 徐飞 

机构地区：[1]兰州城市学院化学与环境科学学院,甘肃兰州730070 [2]兰州大学化学化工学院,甘肃兰州730030

出　　处：《化学研究与应用》2014年第8期1195-1199,共5页Chemical Research and Application

基　　金：甘肃省城市发展研究院项目(2012-GSCFY-KJ04)资助

摘　　要：用荧光、紫外光谱、分子对接研究了柚皮苷与人血清白蛋白(HSA)在pH=7.40的Tris-HCl缓冲溶液中相互作用的情况。结果表明,柚皮苷对人血清白蛋白的内源荧光有明显的猝灭作用,猝灭过程为动态猝灭。根据Stern-Volmer方程计算得到柚皮苷与HSA在293、298和310 K下的结合常数分别为2.472×105、2.210×105和1.392×104L·mol-1,结合位点数约为1。由实验计算出热力学参数焓变ΔH为-16.8 kJ·mol-1,ΔS为46.0 J·mol-1·K-1,推断出柚皮苷与人血清白蛋白之间主要靠疏水作用和静电引力结合,与分子模拟的结果相同。同时采用同步荧光技术考察了柚皮苷对HSA构象的影响。The interaction between naringin and human serum albumin（HSA）in buffer solution（pH=7. 40）were studied by fluores-cence spectroscopy,UV absorption spectroscopy,molecular modeling. It was found that naringin quenched the fluorescence of HSA via a dynamic quenching process. According to the modified Stern-Volmer equation, the binding constants between naringin and HSA at different temperatures（293,298,310 K）were 2. 47×105、2. 21×105 和1. 39×104 L·mol-1respectively,and number of bind-ing sites were 1,which indicated the strong binding between naringin and HSA. The thermodynamic parameters,enthalpy change （ ΔH ） and entropy change（ ΔS ） for the reaction were calculated to be-16. 8 kJ·mol-1 and 46. 0 J·mol-1·K-1 according to van’t Hoff equation. These dates indicated that hydrophobic and electrostatic interactions played a major role in the binding of naringin and HSA,which was in good agreement with molecular modeling studies. Synchronous fluorescence spectroscopy was used in the study of the effect of naringin on the configuration of HSA.

关 键 词：柚皮苷 人血清白蛋白 相互作用 光谱 分子对接 

分 类 号：O641.3[理学—物理化学]