作　　者： ; ;

机构地区： 南昌大学生命科学与食品工程学院食品科学与技术国家重点实验室

出　　处： 《南昌大学学报（理科版）》 2008年第4期377-381,共5页

摘　　要： 用荧光分光光度法和紫外可见分光光度法研究了新型抗高血压药吲达帕胺(Indapamide,IDP)与牛血清白蛋白(BSA)的相互作用机理。结果表明,IDP对BSA的荧光猝灭过程是一个静态猝灭过程,结合常数K=1.29×105L.mol-1,结合位点数n=0.56(27℃)。通过热力学方程,算得焓变ΔH<0,熵变ΔS<0,表明两者之间的作用力主要是氢键和范德华力。基于F rster能量转移理论确定了IDP与BSA的结合距离以及能量转移效率。本实验采用同步荧光光谱法分析了IDP对BSA构象的影响。此外,讨论了Cu2+对IDP与BSA结合反应的影响。 The interaction between indapamide （IDP） and human serum albumin （BSA） has been studied by UV and fluorescence spectral methods. The results of the experiments indicated that the quenching mechanism of fluorescence of BSA by IDP was a static quenching procedure,and the equilibrium constant and the number of binding sites at 27 ℃ were K = 1.29 × 10^5 L · mol^-1 and n =0.56,respectively. The binding distance between IDP and BSA and the energy transfer efficiency were obtained based on the theory of F？ rster spectroscopy energy transfer. The effect of IDP on the conformation of BSA was also investigated by using synchronous fluorescence spectroscopy. The enthalpy change and the entropy change were calculated to be △H 〈 0 and △S 〈 0 , which indicated that hydrogen bonding and van der Waals forces played major role the in interaction between IDP and BSA. In this work,the interaction between IDP and BSA in the presence of copper （ Ⅱ ） was also explored.

关 键 词： 吲达帕胺 牛血清白蛋白 铜离子 光谱法

领　　域： [理学] [理学]