摘要
运用荧光及紫外-可见吸收光谱法研究了胡椒酸丁二醇单酯(简称BPM)与牛血清白蛋白(BSA)的相互作用。实验结果表明,胡椒酸丁二醇单酯与BSA形成基态复合物导致BSA内源性荧光猝灭,猝灭机理主要为静态猝灭和非辐射能量转移,其猝灭速率常数为Kq为1.077×1013L/(mol.s)(25℃)、0.946×1013L/(mol.s)(37℃)。利用荧光猝灭反应测得结合常数KA为2.6×106(25℃)、3.4×106(37℃),结合位点数n为1.30(25℃)、1.33(37℃)。根据Frster能量转移理论得到结合距离r=2.92nm(25℃)、2.66nm(37℃)和能量转移效率E=0.45(25℃)、0.43(37℃)。通过热力学参数计算,确定胡椒酸丁二醇单酯与BSA的相互作用是熵增加和吉布斯自由能降低的自发过程,主要作用力是疏水作用力。
The interaction between butanediol piperinie mono-ester and bovine serum albumin (BSA) has been studied by fluorescence spectroscopy and UV-vis absorption spectroscopy. The experimental results showed that the fluorescence quenching of BSA by butanediol piperinie mono-ester was due to the formation of butanediol piperinie mono-ester-BSA complex through both static quenching and nonradiative energy transfer. The quenching constants (Kq) were 1. 077 × 10^13L/( mol. s) (25 ℃ ) and 0. 946 × 10^13L/( mol. s) (37 ℃ ). With the fluorescence quenching method, the binding constants( KA ) were 2.6 × 10^6L/moL(25℃ )and 3.4 × 10^6L/moL (37 ℃ ), and the values of binding sites (n) were 1.30 (25 ℃ ) and 1.33 (37℃). According to the FSrster theory of non-radiation energy transfer, the b energy transfer efficiencies ( E ) were inding distance(r) were 2.92nm(25℃ ) and 2.66nm(37℃ ), and the 0. 45 ( 25℃ ) and 0. 43 ( 37℃ ). The binding process of binding was a spontaneous molecular interaction in which entropy increased and Gibbs free energy decreased, indicating that the hydrophobic force played major role in the interaction of butanediol piperinie mono-ester and BSA.
出处
《分析试验室》
CAS
CSCD
北大核心
2012年第3期7-10,共4页
Chinese Journal of Analysis Laboratory
基金
国家自然科学资助项目(No.30160103)资助
关键词
胡椒碱
胡椒酸丁二醇单酯
牛血清白蛋白
荧光光谱法
Piperine
Butanediol piperine mono-ester
Bovine serum albumin
Fluorescence spectroscopy