摘要
荧光光谱法和动态光散射法研究大豆苷与牛血清白蛋白在生理条件下的相互作用.研究表明,大豆苷与牛血清白蛋白能形成2∶l复合物,荧光猝灭属于静态猝灭过程;大豆苷与牛血清白蛋白分子间主要的结合作用力为疏水作用;310K下,两者结合常数和结合位点数分别为7.4×l04L·mol―1和1.75;大豆苷使牛血清白蛋白的构象发生了变化;动态光散射数据探讨了牛血清白蛋白与大豆苷分子产生聚集与之相互作用,进一步证实了牛血清白蛋白在大豆苷水溶液中的构象变化.实验结果为进一步研究大豆苷对心血管疾病的药理作用,特别是对血浆蛋白构象的影响提供了重要依据.
The interaction between daidzin and bovine serum albumin （BSA） has been studied with fluorescence spectrum, dynamic light scattering （DLS） under physiological conditions. The experimental results demonstrated that the combination reaction of daidzin with BSA was a static quenching process because of forming a 2 ： 1 complex. And the dominant binding force was hydrophobic interaction. At 310 K, the binding constant and the number of binding sites were 7.4 × 10^4 L·mol^-1 and 1.75, respectively. And the conformation of BSA was changed due to the presence of daidzin. Furthermore, the DLS data suggested that aggregation between BSA and daidzin molecules could render the interactions with them. It was also demonstrated that conformation of BSA was changed in daidzin aqueous solution. These provide important information for the study of cardiovascular pharmacological effects of daidzin and the influence of daidzin on the configuration change of BSA.
出处
《化学学报》
SCIE
CAS
CSCD
北大核心
2009年第14期1609-1614,共6页
Acta Chimica Sinica
基金
陈可冀中西医结合发展基金暨福建省高校中药学重点实验室开放课题基金(No.ckj2008029)资助项目
关键词
激光光散射
荧光光谱
大豆苷
牛血清白蛋白
聚集态
laser light scattering
fluorescence spectrum
daidzin
bovine serum albumin
aggregation
