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Vol. 25 No. 4 (2013): Vol 25 Issue 4

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Transition Metal Ion Chelating of Some Coumarin Antioxidants and the Interaction with Bovine Serum Albumin

https://doi.org/10.14233/ajchem.2013.13791
Ye Zhang
School of Chemistry and Chemical Engineering, South Central University, Hunan 410083, P.R. China ; Department of Chemistry, Guilin Normal College, Guangxi 541001, P.R. China
Biqun Zou
Department of Chemistry, Guilin Normal College, Guangxi 541001, P.R. China
Yilin Fang
Department of Chemistry, Guilin Normal College, Guangxi 541001, P.R. China
Zhenghong Pan
Guangxi Key Laboratory of Functional Phytochemicals Research and Utilization, Guangxi Institute of Botany, Guilin 541006, P.R. China
Xianghui Yi
Department of Chemistry, Guilin Normal College, Guangxi 541001, P.R. China
Dianpeng Li
Guangxi Key Laboratory of Functional Phytochemicals Research and Utilization, Guangxi Institute of Botany, Guilin 541006, P.R. China

Corresponding Author(s) : Xianghui Yi

yixianghui2008@yahoo.com.cn

Asian Journal of Chemistry, Vol. 25 No. 4 (2013): Vol 25 Issue 4

Abstract

To investigate whether the coumarins antioxidants 1-14 may exert their antioxidant effect through transition metal ion chelation, the copper and ferrous chelating properties with coumarins were studied. It was found from fluorescence spectra that the binding constants Ka of coumarins 1-14 were in the range of 1.25 × 103 to 4.46 × 105 M-1, which indicated that the transition ion chelation play an important role in their antioxidant abilities. The interaction of coumarins 1-14 with bovine serum albumin was also studied by fluorescence spectra, since that the interaction of drugs with bovine serum albumin may have important influence on the drugs' pharmacology and pharmacodynamics. The results showed that the probable mechanism of the coumarins 1-14 interaction with bovine serum albumin was a static process and the binding constants Ka were 5.96 × 104 to 5.22 × 106 M-1, demonstrating a strong binding between coumarins 1-14 and bovine serum albumin. In addition, the binding numbers of coumarins 1-14 with transition metal ion and bovine serum albumin were determined to be 1, respectively, suggesting that each unit of coumarins 1-14 can bind with a unit of transition metal ion and a unit of bovine serum albumin. All the results may provide important information for the rational design of other analogous new antioxidants and drugs.

Keywords

Coumarin antioxidants Transition metal ion chelation Bovine serum albumin Fluorescence spectra
Zhang, Y., Zou, B., Fang, Y., Pan, Z., Yi, X., & Li, D. (2012). Transition Metal Ion Chelating of Some Coumarin Antioxidants and the Interaction with Bovine Serum Albumin. Asian Journal of Chemistry, 25(4), 2265–2269. https://doi.org/10.14233/ajchem.2013.13791
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