Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique
Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique
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DOI：
10.1016/j.jlumin.2011.08.014
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发表时间：
2012-01-01
影响因子：
3.6
通讯作者：
Wang, Yu
中科院分区：
文献类型：
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作者：
Bi, Shuyun;Yan, Lili;Wang, Yu
用荧光猝灭法、同步荧光法和紫外-可见吸收光谱法研究了3种黄酮类化合物：柚皮素、橙皮素和芹菜素在pH 7.4时与牛血清白蛋白(BSA)的结合。结果表明，柚皮素、橙皮素和芹菜素对牛血清白蛋白的内源荧光有较强的猝灭作用。Stern-Volmer曲线表明，这些淬火过程均为静态淬火过程。在291K时，结合常数K-A((柚皮苷))=4.08×10(4)<；K-A((橙皮素))=5，40×10(4)近似于K-A((芹菜素))=5.32×10(4)L摩尔(-1)。黄酮类化合物与牛血清白蛋白的结合主要是疏水作用力和静电作用力。根据Forster非辐射能量转移理论，得到柚皮素-BSA、橙皮素-BSA和芹菜素-BSA的结合距离(r(0))分别为3.36、3.47和3.30 nm。并详细研究了Fe3+、Cu2+、Mg2+、Mn2+、Zn2+、Ca2+等常见离子对结合的影响。还进行了竞争结合。表观结合常数(K‘(A))表明，在BSA溶液中，一种黄酮类化合物对另一种黄酮类化合物与蛋白质的结合有明显的影响。(C)2011爱思唯尔B.V.保留所有权利。
The three flavonoids including naringenin, hesperetin and apigenin binding to bovine serum albumin (BSA) at pH 7.4 was studied by fluorescence quenching, synchronous fluorescence and UV-vis absorption spectroscopic techniques. The results obtained revealed that naringenin, hesperetin and apigenin strongly quenched the intrinsic fluorescence of BSA. The Stern-Volmer curves suggested that these quenching processes were all static quenching processes. At 291 K, the value and the order of the binding constant were K-A ((naringenin))=4.08 x 10(4) < K-A ((hesperetin))=5,40 x 10(4) approximate to K-A ((apigenin))=5.32 x 10(4) L mol(-1). The main binding force between the flavonoid and BSA was hydrophobic and electrostatic force. According to the Forster theory of non-radiation energy transfer, the binding distances (r(0)) were obtained as 3.36, 3.47 and 3.30 nm for naringenin-BSA, hesperetin-BSA and apigenin-BSA, respectively. The effect of some common ions such as Fe3+, Cu2+, Mg2+, Mn2+, Zn2+ and Ca2+ on the binding was also studied in detail. The competition binding was also performed. The apparent binding constant (K'(A)) obtained suggested that one flavonoid had an obvious effect on the binding of another flavonoid to protein when they coexisted in BSA solution. (C) 2011 Elsevier B.V. All rights reserved.