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2012 , Vol. 70 >Issue 12: 1379 - 1384

DOI: https://doi.org/10.6023/A1112156

研究论文

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

  • 张方圆 ,
  • 倪永年
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  • a 南昌大学食品科学与技术国家重点实验室 南昌 330047;
    b 南昌大学化学系 南昌 330031

收稿日期: 2011-12-15

  修回日期: 2012-03-19

  网络出版日期: 2012-04-06

基金资助

国家自然科学基金(No. 21065007)和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.

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

  • Zhang Fangyuan ,
  • Ni Yongnian
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  • a State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047;
    b Department of Chemistry, Nanchang University, Nanchang 330031

Received date: 2011-12-15

  Revised date: 2012-03-19

  Online published: 2012-04-06

Supported by

Project was supported by the National Natural Science Foundation of China (No. 21065007) and the State Key Laboratory of Food Science and Technology of Nanchang University (Nos. SKLFMB-200807, SKLF-TS-200919).

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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105 L/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.

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

本文引用格式

张方圆 , 倪永年 . 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[J]. 化学学报, 2012 , 70(12) : 1379 -1384 . DOI: 10.6023/A1112156

Abstract

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 (DH, DS, and DG) 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.

Key words： β-carotene; Sunset yellow; bovine serum albumin; molecular spectrometry; CD

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