A study of the binding of CI Mordant Red 3 with bovine serum albumin using fluorescence spectroscopy

被引：94

作者：

Ding, Fei ^{[1
]}

Huang, Jinli ^{[1
]}

Lin, Juan ^{[2
]}

Li, Zhiyuan ^{[1
]}

Liu, Feng ^{[1
]}

Jiang, Zhiqiang ^{[3
]}

Sun, Ying ^{[1
]}

机构：

[1] China Agr Univ, Dept Chem, Beijing 100193, Peoples R China

[2] China Univ Min & Technol, Dept Chem, Xuzhou 221116, Peoples R China

[3] Panzhihua Univ, Coll Biol & Chem Engn, Panzhihua 617000, Peoples R China

来源：

DYES AND PIGMENTS | 2009年 / 82卷 / 01期

关键词：

Bovine serum albumin; CI Mordant Red 3; Fluorescence spectroscopy; LW-vis absorption spectrum; Fluorescence resonance energy transfer; Thermodynamic parameter; STRUCTURAL FLUCTUATIONS; OPTICAL SPECTROSCOPY; PROTEIN FLUORESCENCE; TOXICITY; OXYGEN; HYDROCHLORIDE; MECHANISM; ACID;

D O I：

10.1016/j.dyepig.2008.11.003

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The interaction of C.I. Mordant Red 3 and bovine serum albumin was investigated using fluorescence and UV-vis absorption spectroscopy. Fluorescence quenching, from which binding parameters were evaluated, revealed that the quenching of the serum by C.I. Mordant Red 3 resulted from the formation of a dye-serum complex. The enthalpy and entropy changes for the reaction were -50.49 kJ mol(-1) and -50.88 J mol(-1) K-1 respectively. van der Waals forces and hydrogen bonds were the dominant intermolecular forces that stabilize the complex: the distance between donor and acceptor was 2.79 nm, according to Forster's non-radiative energy transfer theory. The effect of the dye upon the conformation of bovine serum albumin was analyzed using synchronous fluorescence spectrum. (c) 2008 Elsevier Ltd. All rights reserved.

引用

页码：65 / 70

页数：6

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