日落黄和β-胡萝卜素与牛血清白蛋白相互作用的对比研究  

A Comparison Study on the Interaction of Sunset Yellow and β-Carotene with Bovine Serum Albumin

作　　者：张方圆[1,2] 倪永年[1,2] 

机构地区：[1]南昌大学食品科学与技术国家重点实验室,南昌330047 [2]南昌大学化学系,南昌330031

出　　处：《化学学报》2012年第12期1379-1384,共6页Acta Chimica Sinica

基　　金：国家自然科学基金(No.21065007);南昌大学食品科学与技术国家重点实验室基金(Nos.SKLFMB-200807;SKLF-TS-200919)资助项目~~

摘　　要：在模拟生理pH条件(pH=7.4)下,采用多种光谱法研究日落黄和β-胡萝卜素与BSA的相互作用,并比较两者与BSA相互作用过程的差异性.通过荧光光谱法和紫外吸收光谱法确定了日落黄和β-胡萝卜素对牛血清白蛋白的荧光猝灭机制,采用Stern-Volmer、双对数方程和热力学公式求出相互作用的猝灭常数、结合常数Ka、结合位点数n和作用力类型.结果表明:日落黄和β-胡萝卜素对BSA的猝灭属于静态猝灭,两者与BSA的Ka都达到105L/mol,结合位点数均为1,日落黄与BSA的作用力以静电引力为主,而β-胡萝卜素则是通过氢键和范德华力与BSA作用.通过红外光谱法和圆二色谱法研究了二者对BSA构象的影响,结果表明,日落黄与BSA作用的过程中,会引起BSA二级结构的改变,而β-胡萝卜素则对BSA的构象基本不产生影响.Interaction of Sunset yellow （SY） and β-carotene （BC） with bovine serum albumin （BSA） was investigated under simulated physiological conditions by spectroscopic approaches （fluorescence, UV-Vis, FT-IR and CD）. Both SY and BC quenched the intrinsic fluorescence of BSA through static quenching mechanism. The thermodynamic parameters （△H, △S, and △） obtained from the fluorescence data measured at three different temperatures indicated that the binding of SY to BSA involved electrostatic force, and that of BC to BSA mainly by hydrogen bonding and van der Waals forces. The binding sites number n and binding constants Ka were also obtained. The result of FT-IR spectra and CD showed that the binding of SY to BSA induced conformational changes in BSA.

关 键 词：Β-胡萝卜素 日落黄 牛血清白蛋白 分子光谱法 圆二色谱法 

分 类 号：R96[医药卫生—药理学]